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HERMAN MORITZ KALCKAR
March 26, I908-May I 7, 199'
BY EUGENE P. KENNEDY
HERMAN MORITZ KAECKAR died in Cambridge, Massachu-
setts, on May 17, 1991, at the age of eighty-three. His
scientific career spanner! much of the perioc! of clevelop-
ment of moclern biochemistry, to which he macle contribu-
tions of central importance.
Kalckar was born in Copenhagen on March 26, 190S,
into a family he clescribec! in an autobiographical essay as
having been micicIle-ciass Jewish-Danish for many genera-
tions. Kalckar's broac! interests in literature en c! the arts
hac! their origins in his early family life. His mother, Bertha
Rosalie Melchior KaTckar, react wiclely in French en c! Ger-
man as well as Danish literature. His father, Lucivig Kalckar,
a businessman, was clevotec! to music en c! the theater. Lucivig
KaTckar attenclec! the woric! premiere of Ibsen's "A Doll's
House" at the Royal Theater in Copenhagen in November
IS79 and later wrote an enthusiastic review of it. Herman
KaTckar tracer! some of his own enthusiasm for music, en c!
in particular for Mozart, to his father's example.
Herman's younger brother, Fritz Kalckar, was a giftec!
physicist en c! a colleague en c! protege of Niels Bohr. The
death of Fritz in 1938 at twenty-eight years of age was a
devastating blow for the entire family.
149
OCR for page 150
50
B I O G RA P H I C A L
EMOIRS
KaTckar receiver! his early schooling in the Ostre Borgerclyc!
Skole, locater! within an easy walk of his home in Copenhagen.
The headmaster, I. L. Heiberg, was a Greek scholar of inter-
national repute, en c! KaTckar pair! tribute to the "Athenian
flavor" of the school. He felt a special gratitude to the phys-
ics teacher, H. C. Christianson, whom he recallec! many years
later as a formiciable en c! passionately clevotec! teacher.
Kalckar completec! his studies for a degree in medicine
at the University of Copenhagen in 1933 en c! then began
his scientific career in 1934 as a cancliciate for the Ph.D.
degree in the Department of Physiology under the direc-
tion of Ejnar LuncisgaarcI. Luncisgaarc! hac! earlier macle
the important fincling that frog muscles poisoner! with
iocloacetate en c! therefore unable to carry out glycolysis (the
splitting of glucose to lactic acicI) are nevertheless capable
of carrying out a limiter! number of contractions. Luncisgaarc!
later shower! that these "nonIactic" contractions were at the
expense of the clephosphorylation of creating phosphate,
which hac! been cliscoverec! en c! characterizec! only a few
years earlier by Cyrus Fiske at the Harvarc! Meclical School.
In 1932 Fritz Lipmann, unable to work in Nazi Germany,
mover! to Copenhagen, where he was closely associates! with
LuncisgaarcI. Lipmann became one of Kalckar's mentors en c!
a close friend, a relationship that was to be lifelong. Lipmann
was already deeply interested not only in Lundsgaard's work
on the role of phosphate esters in muscle contraction but
also in the biological functions of phosphorylation reac-
tions more generally. In his masterly and highly influential
review in 1941 Lipmann was to emphasize the central role
of aclenosine triphosphate (ATP) as an "energy-rich" phos-
phate ester, the breakdown of which to aclenosine cliphos
phate (ADP) and inorganic phosphate (Pi) drives not only
muscle contraction but also a host of other energy-requir-
ing processes. Because the cell has a limiter! supply of ATP,
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HERMAN MORITZ KALCKAR
151
the ADP former! by its breakdown must be continuously
rephosphorylatec! to AT P. In muscle this may be clone by
use of creating phosphate, a cellular reserve of "energy-rich
phosphate" that is present, however, only in limiter! amounts.
At that time the only primary source of energy known to
biochemists for the rephosphorylation of ADP to ATP was
the splitting of glucose to lactic acid in muscle or in yeast
to alcohol en c! carbon clioxicle. The brilliant achievements
of Otto Warburg (which both Kalckar en c! Lipmann greatly
acimirecI) hac! reveaTec! the reactions by which ADP is phos-
phorylated to ATP during glycolysis.
Glycolysis, however, is a process that can occur anaerobi-
cally in the absence of molecular oxygen. Classic investiga-
tions by Pasteur hac! macle it clear that aerobic metabolism
of glucose by yeast is vastly more energy efficient than the
anaerobic process. How is energy captures! by the oxicia-
tion of sugars en c! other foodstuffs linker! to the recluction
of molecular oxygen? This was the question confronted by
KaTckar as he began the investigations in the period 1937
39 that lee! him to the demonstration that cell-free extracts
of kiciney cortex catalyze oxiciative phosphorylation that
is, the formation of ATP in reactions strictly clepenclent on
the recluction of oxygen en c! inclepenclent of glycolysis. An
important technical point in these experiments was the use
of soclium fluoride to inhibit interfering phosphatases that
otherwise wouIc! break clown ATP en c! other phosphate es-
ters almost as soon as they were formed.
As is now well known, aerobic nonphotosynthetic organ-
isms, inclucling ourselves, derive vastly more metabolic en-
ergy from oxiciative phosphorylation than from any other
source. It is estimates! that the complete utilization of glu
cose in muscle leacis to the procluction of about seventeen
times more ATP via oxidative phosphorylation than is pro-
duced in anaerobic glycolysis. Oxidative phosphorylation is
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152
B I O G RA P H I C A L
EMOIRS
therefore a process of central bioenergetic importance. It
became (anc! still is) the object of intensive studies in many
laboratories throughout the worIcI. Localizec! in the inner
membrane of the mitochoncirion, oxiciative phosphoryla-
tion prover! extraorclinarily resistant to biochemical clissec-
tion. Two clecacles were to pass before real insight was gainer!
into the mechanism of oxiciative phosphorylation with the
clevelopment by Peter Mitchell of the chemiosmotic theory.
To this ciate many important features of oxiciative phos-
phorylation remain imperfectly unclerstoocI, but KaTckar's
work openec! the way to its systematic exploration.
At about the same time as Kalckar's experiments V. A.
Belitzer, working in virtual isolation in the Soviet Union,
macle similar observations on oxiciative phosphorylation in
experiments on preparations clerivec! from pigeon breast
muscle. Although Belitzer's work clic! not become known in
western Europe until a consiclerable time after Kalckar's
first publications, it was characteristic of Kalckar that he
was always generous in acknowleciging Belitzer's contribu-
tion. During his trip to the Soviet Union in 1960 Kalckar
looker! up Belitzer in Kiev en c! took some pains to make
arrangements to be photographer! with him.
Kalckar's early experiments on oxidative phosphorylation
also provided evidence for the production of phospho-
enolpyruvate from fumaric or maTic acids, observations that
later proviclec! an important clue to the mechanisms in-
volvec! in the formation of glucose from noncarbohycirate
sources in animal tissues.
Kalckar later wrote an interesting historical account of
the origins of the concept of oxiciative phosphorylation en c!
his early experimental work on this theme (1974~.
In 1939, having completer! his work for the Ph.D. degree,
Kalckar was appointed a Rockefeller research fellow for a
year of postcloctoral stucly at the California Institute of Tech
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HERMAN MORITZ KALCKAR
153
nology. On his trip across the Uniter! States he stopper! at
the famous laboratory of Gerty en c! Car! Cori at Washing-
ton University in St. Louis, then one of the few centers of
the "new biochemistry" in the Uniter! States. There he fount!
Siciney Colowick, then a graduate student, attempting to
duplicate Kalckar's experiments on oxidative phosphoryla-
tion, without success. Colowick, untrainec! in the methods
introclucec! by Warburg en c! follower! by Kalckar, hac! been
simply incubating tissue extracts in test tubes without pro-
vicling for the efficient diffusion of oxygen into them. Thirty-
five years later Colowick summarizer! Kalckar's helpful acI-
vice: "'Shake it!' sail! Dr. K., en c! everything was OK!"
KaTckar's stay in California allowed! him to take the fa-
mous microbiology course in Pacific Grove taught by C. B.
van Niel, whose insight into the unclerlying unity of the
biochemistry of living organisms en c! charismatic personal-
ity macle a creep impression on Kalckar, as on so many oth-
ers. This experience may have planter! a seer! that lee! later
to KaTckar's interest in microbial molecular biology.
During his stay in Pasadena, with the encouragement of
Linus Pauling, Kalckar undertook the preparation of a com-
prehensive review of bioenergetics with emphasis on the
role of phosphate esters in energy transduction. Its publica-
tion (1941) clic! much to advance the new icleas that he en c!
· ~
L~pmann were pursuing.
In ~ 940 Kalckar acceptec! an appointment as research
fellow in Cori's Department of Pharmacology at Washing-
ton University. The invasion of Denmark by the Nazis in
the spring of 1940 hac! macle it impossible for Kalckar en c!
his wife, Vibeke, to return to Copenhagen, en c! Kalckar was
fortunate to have the opportunity to spenc! the next three
years in a stimulating en c! productive environment with con-
genial colleagues. He joiner! forces with Siciney Colowick.
Their work lee! them to the discovery in muscle extracts of
OCR for page 154
54
B I O G RA P H I C A L
EMOIRS
a remarkable enzyme, namer! myokinase by them, but now
more precisely caller! aclenylate kinase, that catalyzes the
following reaclily reversible reaction:
ATP + AMP
2 ADP (~y
Many biological processes leac! to the production of acI-
enosine monophosphate (AMP), which, however, cannot be
phosphorylated to ATP during oxidative phosphorylation
or glycolysis, processes that are specific for ADP as phos-
phate acceptor. In the absence of reaction all, which "res-
cues" AMP by converting it to ADP, all of the aclenine nucle-
oticles of the cell wouic! be irreversibly converter! to AMP.
Later experiments by other workers shower! that mutations
that block the activity of aclenylate kinase are lethal to cells
of Escherichia coli.
In 1943 Kalckar was appointee! research associate at the
Public Health Institute of the city of New York. One of the
attractions of the post was a laboratory equipped with a
new ultraviolet spectrophotometer, then still a rather rare
instrument. Kalckar clevelopec! spectrophotometric meth-
ocis for the stucly of the metabolism of nucleosicles en c!
nucleoticles, the builcling blocks of RNA en c! DNA. It hac!
earlier been reporter! by Klein that the enzymic hycirolysis
of nucleosicles is stimulates! by the aciclition of phosphate
or arsenate. Coming from the Cori laboratory, the center
of work on glycogen phosphorylase, Kalckar realized the
possible significance of the role of phosphate en c! soon
macle the important discovery that the phosphorolytic cleav-
age of nucleosides is similar to that of glycogen.
r~oose-hypoxanth~ne + Pi
. . .
ribose-~-P + hypoxanthine
(2)
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HERMAN MORITZ KALCKAR
155
The reaction is reacliTy reversible. IncleecI, the equilibrium
position lies to the left of Equation (2) as written, favoring
the synthesis of the nucleosicle rather than its breakdown.
As the first demonstration of the enzymic synthesis of a
nucleosicle, this work attracted! consiclerable attention. It
must be recalled! that in 1945, when this work was clone,
very little was known of the metabolism of nucleic acids or
incleec! of their functions in living cells. Later work was to
show that nucleosicle phosphorylases function as "salvage
enzymes" in the clegraciation rather than the synthesis of
builcling blocks of nucleic acid.
In 1946 Kalckar returned to Copenhagen, where a new
laboratory was set up for him with the support of Ejnar
Luncisgaarc! en c! with financial backing from American as
well as Danish sources. The principal theme of research at
the new "Cytofysiologisk Institute" was the metabolism of
nucleosides and nucleotides. Kalckar attracted gifted young
collaborators, such as Hans Klenow, Morris Friec~kin, en c!
Walter McNutt, en c! the laboratory became a leacling center
for work in this fielcI.
In 1952 Kalckar began his studies on the metabolism of
galactose in microbial en c! animal tissues. This became a
principal pursuit after his move to the National Institutes
of Health in 1952, first as a visiting scientist en c! later with a
permanent appointment at the National Institute of Arthri-
tis en c! Metabolic Diseases.
In mammals the utilization of galactose, a component of
milk sugar en c! therefore a major constituent in the cliet of
infants, begins with its phosphorylation to galactose-~-P, which
then must be converted to glucose-~-P, the further metabo-
lism of which occurs by well-known reactions. The pioneer-
ing work of Luis Leloir lee! to the discovery of the central
role of uricline cliphosphate derivatives in the interconversion
of galactose en c! glucose, sugars that are epimers, that is,
OCR for page 156
56
BIOGRAPHICAL MEMOIRS
differing in configuration only at a single carbon atom (C-
4~. Leloir shower! that the two sugars are interconvertec! in
the form of their uricline cliphosphate derivatives as in Equa-
tion (4), catalyzer! by an epimerase, en c! suggester! that the
synthesis of uridine diphosphate galactose (galactose-~-P-P-
uricline~ might take place by reaction ~3):
galactose-~-P + glucose-~-P-P-uridine
~alactose-~-P-P-uricline + ~lucose-~-P (3)
a
a
NAD
galactose-~-P-P-uridine
glucose-~-P-P-uridine
(4)
In the sum of (3) en c! (4) the uricline-linkoc! forms of the
sugars cancel out, en c! the overall reaction is:
galactose-~-P glucose-~-P (3 + 4)
In 1953 Kalckar en c! his collaborators reporter! direct evi-
dence that the synthesis of uridine diphosphate galactose
floes in fact occur in extracts of the yeast Saccharomyces Francis
by reaction (3), catalyzed by the enzyme galactose-~-P uridyly!
transferase. They also fount! an alternative reaction for the
synthesis of uricline cliphosphate galactose in yeast:
galactose-~-P + P-P-P-uridine
galactose-~-P-P-uridine + P-P
(5)
It is important to note that reaction (5) floes not occur in
human tissues, in which reaction (3), catalyzed by the uridyly!
transferase, is an essential step in the utilization of galac-
tose as an energy source.
KaTckar clevisec! a methoc! to determine the levels of the
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HERMAN MORITZ KALCKAR
157
uriclyly! transferase catalyzing reaction (3) in Tysates of rec!
blooc! cells, employing his favorite spectrophotometric ap-
proach. At just this time Kurt Isselbacher was also at NIH,
carrying out research in collaboration with Gordon Tomkins
en c! Julius AxeIrocI. As part of his clinical duties, Isselbacher
was treating a chilc! whom he cliagnosec! as suffering from
galactosemia, a severe inheritec! clisorcler characterizec! by
the inability to break down galactose, which leads to accu-
mulation of high levels of galactose in blooc! en c! tissues.
Isselbacher sought out KaTckar, en c! a collaboration was be-
gun that soon lee! to the fincling that the enzyme defect in
the most serious form of human galactosemia is in the uriclyly!
transferase that catalyzes reaction (3~. This in turn lee! to
the clevelopment of a simple test for the presence or ab-
sence of this enzyme in rec! blooc! cells that is now wiclely
user! to screen newborn infants for galactosemia, a disease
that can be effectively treater! by removal of milk en c! other
sources of galactose from the cliet. The clevelopment of this
test was of great practical consequence since early diagnosis
is vital to prevent severe mental retardation en c! other cle-
velopmental defects.
In 1958 KaTckar acceptec! a professorship in the Depart-
ment of Biology of Johns Hopkins University. This year also
market! the publication of his highly original proposal that
the contamination of foodstuffs from the fallout following
atmospheric tests of nuclear weapons conic! be measurer!
by the analysis of the content of strontium-90 in the milk-
teeth of young chiTciren. As he pointer! out, measurement
of racliation from clecicluous incisor teeth wouIc! reveal the
levels of isotope ingestec! about seven years previous to shecI-
cling of the teeth, when the caTcifiec! structure of the teeth
had been deposited. By this proposal Kalckar hoped to fo-
cus attention in a dramatic way on the pollution of the
environment by tests of nuclear weapons. The iclea attracted!
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58
B I O G RA P H I C A L
EMOIRS
consiclerable attention, en c! extensive collections of milk-
teeth were in fact macle, particularly by a group of researchers
at Washington University in St. Louis. It was learner! that
milk-teeth from chiTciren born in 1956 container! about ten
times more strontium-90 than teeth from chilciren born in
1950. Fortunately, after the ban on atmospheric testing the
levels fell once again to Tower levels.
In 1961 Kalckar mover! to the Harvarc! Meclical School as
professor of biological chemistry ant! heat! of the Biochemical
Research Laboratory of Massachusetts General Hospital
(MGH). He succeeclec! Fritz Lipmann in that position. Here
he continues! his studies on the metabolism of galactose in
animal tissues with special attention to the epimerase that
catalyzes reaction (4) above.
Kalckar now also became cleeply interested! in the role of
the cell surface in sensory processes en c!
in cell signaling
en c! often referrer! to this fielcI, then newly emerging, as
"ektobiology." Winfriec! Boos, his young colleague at MGH,
carrier! out an intensive stucly of the transport of galactose
into cells of E. coil, which culminates! in the isolation en c!
cletailec! characterization of a specific galactose-bincling pro-
tein that was shown to be an essential part of the transport
system. Julius Adler and his colleagues at the University of
Wisconsin cliscoverec! at about the same time that cells of E.
cold can detect the presence of galactose in the meclium en c!
"chase" this sugar by a positive chemotactic response. Kalckar
immecliately suggester! that the galactose-bincling protein
that could "recognize" galactose for transport might also be
needler! for the chemotactic response. The first tests of this
notion, however, were clisappointingly negative. Kalckar per-
sistec! in his iclea, however, ant! further experiments reveaTec!
that an unexpected complexity of the transport system had
renclerec! the first tests invalicI. The final definitive experi-
ments reveaTec! that the bincling protein plays a vital role
OCR for page 159
HERMAN MORITZ KALCKAR
159
not only in the transport of galactose but also in chemot-
axis, an outcome that gave Kalckar consiclerable satisfac-
tion.
KaTckar was also greatly interested! in the conversion of
galactose to cell-surface lipopolysaccharicles in bacteria, work
vigorously pursues! in his MGH laboratories by Hiroshi
Nikaiclo. Nikaiclo's pioneering studies on the biosynthesis
of lipopolysaccharide in Salmonella employed both genetic
en c! biochemical approaches en c! clic! much to clarify the
complex reaction sequences, particularly the role of lipicI-
linkoc! intermediates.
Kalckar turner! next to the problem of the regulation of
the transport of sugars into mammalian cells en c! the im-
portance of this process in tumor cells. This work was in
part stimulates! by a collaborative study in 1973 with Sen-
itiroh Hakomori at the University of Washington in Seattle
on carbohydrate utilization en c! the uptake of galactose in
hamster cells transformer! by polyoma virus.
In 1974 KaTckar retiree! as heat! of the Biochemical Re-
search Laboratory but continues! his research as visiting
professor in the Huntington Laboratories at MGH until 1979.
At that time he mover! to the Department of Chemistry at
Boston University as clistinguishec! research professor, an
appointment he greatly valued because it permitted him to
continue his research interests in a new en c! stimulating
environment to the very ens! of his life. The work on hex-
ose transport en c! metabolism in normal en c! malignant cells
continued to be the theme of much of the work in the
laboratory at Boston University en c! the subject of many
papers with his longtime collaborator, Donna Ullrey, the
last of which was publisher! only shortly before his cleath.
Kalckar's achievements in science brought him wicle rec-
ognition, inclucling election to the National Academy of
Sciences, the Royal Danish Academy, and the American Acad
OCR for page 160
60
B I O G RA P H I C A L
EMOIRS
emy of Arts en c! Sciences, as well as honorary degrees from
Washington University, the University of Chicago, en c! the
University of Copenhagen.
To his many friends, KaTckar's character en c! personality
were as impressive as his scientific accomplishments. Through-
out his entire career Kalckar won the affection en c! acimira-
tion of a large number of students en c! junior associates
who were trainee! in his laboratory. The sweep of his intel-
lect was very broacI, his spirit was open en c! generous, en c!
he hac! a wonclerfuT sense of humor. Upon first acquain-
tance many fount! it clifficult to follow the threat! of his
discourse, partly because he was apt to begin a new topic in
medics res without explanatory preamble en c! partly because
he often pair! the listener the compliment of omitting from
a chain of reasoning the links that seemec! obvious. After
one became accustomec! to this style it enhancer! the effect
of his gentle, unclerstatec! wit.
The same enlightenec! humanism that shaper! Kalckar's
tastes in music en c! the arts was evident in his view of woric!
problems, as eviclencec! by his concern for the mounting
threat of nuclear warfare en c! the ciangers of continues!
testing of nuclear weapons, which he hac! ciramatizec! by
the milk-teeth collection project.
Kalckar's first marriage, to the musician Vibeke Meyer,
enclec! in divorce in 1950. Three chiTciren, Sonja, Nina, en c!
Niels, to whom he was cleeply clevotecI, were born of his
second marriage to the developmental biologist Barbara
Wright. After clissolution of that marriage, KaTckar in 1968
marries! the interior designer Agnete Friclericia Laursen,
who survives him. For the last twenty-three years of his life,
Agnete's love and support were an essential part of Herman's
life, en c! their home in Cambridge was a focus of warmth
en c! hospitality for friends en c! colleagues.
OCR for page 161
HERMAN MORITZ KALCKAR
SELECTED BIBLIOGRAPHY
1937
Phosphorylation in kidney tissues. Enzymologia 2:47.
1938
161
Formation of a new phosphate ester in kidney extracts. Nature 142:871.
1939
Coupling between phosphorylations and oxidations in kidney ex-
tracts. Biochem. f. 6:209.
1941
The nature of energetic coupling in biological synthesis. Chem. Rev.
28:71.
With S. P. Colowick. An activator of the hexokinase system. 7. Biol.
Chem. 137:789.
1942
The enzymatic action of myokinase. 7. Biol. Chem. 143:299.
1943
With S. P. Colowick. The role of myokinase in transphosphorylations.
I. The enzymatic phosphorylation of hexoses by adenylpyrophosphate.
f. Biol. Chem. 148: 117.
1944
Spectroscopic microdetermination of muscle adenylic acid. Science
99:131.
1945
Enzymatic synthesis of a nucleoside. 7. Biol. Chem. 158:723.
1947
The enzymatic synthesis of purine ribosides. 7. Biol. Chem. 167:477.
OCR for page 162
162
B I O G RA P H I C A L
1948
EMOIRS
With H. Klenow. Enzymatic transformation of pteroylglutamic acid.
f. Biol. Chem. 172:351.
1949
With M. Friedkin and E. Hoff-Jorgensen. Enzymatic synthesis of
desoxyribose nucleoside with desoxyribose phosphate ester. 7. Biol.
Chem. 178:527.
1952
Enzymatic reactions in purine metabolism. Harvey Lect. Ser. 45, pp.
11-39.
1953
With B. Braganea and A. Munch-Petersen. Uridyl transferases and
the formation of UDP-galactose. Nature 172:1038.
1954
Biosynthesis and metabolism of phosphorus compounds. Annul Rev.
Biochem. 23:527.
With J. L. Strominger, J. Axelrod, and E. Maxwell. Enzymatic oxida-
tion of uridine diphosphate glucose to uridine diphosphate glu-
curonic acid. J. Am. Chem. Soc. 76:6411.
1955
With E. Maxwell and R. M. Burton. Galacto-waldenase and the enzy-
matic incorporation of galactose-l-phosphate in mammalian tis-
sues. Biochim. Biophys. Acta 18:389.
1956
With E. P. Anderson and K. J. Isselbacher. Galactosemia, a congeni-
tal defect in a nucleotide transferase. A preliminary report. Proc.
Natl. A cad . Sci. U. S. A. 42:49.
With K. J. Isselbacher, E. P. Anderson, and K. Kurahashi. Congeni-
tal galactosemia, a single enzymatic block in galactose metabo-
lism. Science 123:635.
1957
Biochemical mutations in man and microorganisms. Science 125:105.
OCR for page 163
HERMAN MORITZ KALCKAR
163
With E. P. Anderson, K. Kurahashi, and K. T. Isselbacher. A specific
enzymatic assay for the diagnosis of congenital galactosemia. I.
The consumption test. 7. Lab. Clin. Med. 50:469.
1958
An international milk teeth radiation census. Nature 182:283.
With E. Maxwell and H. de Robichon-Szulmajster. Yeast uridine
diphosphate galactose-4-epimerase: correlation between activity
and fluorescence. Arch. Biochem. Biophys. 78:407.
1962
With T. A. Sundararajan and A. M. C. Rapin. Biochemical observa-
tions on E. cold mutants defective in uridine diphospho-glucose.
Proc. Natl. Acad. Sci. U.S.A. 48:2187.
1965
Galactose metabolism and cell sociology. Science 150:305.
1968
With A. M. C. Rapin and L. Alberico. The metabolic basis for mak-
ing of receptor sites on E. Coli K12 for C21, a lipopolysaccharide
core-specific phage. Arch. Biochem. 128:95.
1969
Biological Phosphorylations: Development of Concepts. Englewood Cliffs,
N.T.: Prentice-Hall.
With H. C. P. Wu and W. Boos. Role of the galactose transport
system in the retention of intracellular galactose in Escherichia
coli. J. Mol. Biol. 41:109.
1971
The periplasmic galactose binding protein of Escherichia coli. Science
174:557.
1973
With D. Ullrey, S. Kijomoto, and S. Hakomori. Carbohydrate ca-
tabolism and the enhancement of the uptake of galactose in hamster
cells transformed by polyoma virus. Proc. Natl. A cad. Sci. U.S.A.
70:839.
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164
B I O G RA P H I C A L
1974
EMOIRS
Origins of the concept of oxidative phosphorylation. Mol. Cell. Biochem.
5 55
· ~
1975
With T. J. Silhavy and W. Boos. The role of the Escherichia cold galac-
tose-binding protein in galactose transport and chemotaxis. In
Twenty-fifth Mosbacher Colloquium, ed. L. Jacnicke, pp. 1-30. Ber-
lin: Springer-Verlag.
1976
Cellular regulation of transport and uptake of nutrients: an over-
view. 7. Cell. Physiol. 89:503
1985
With P. Plesner and D. B. Ullrey. Mutations in the phosphoglucose
isomerase gene can lead to marked alterations in cellular ATP
levels in cultured fibroblasts exposed to simple nutrient shifts.
Proc. Natl. Acad. Sci. U.S.A. 82:2761.
1986
Autobiographical notes from a nomadic biochemist. In Selected Top-
ics in the History of Biochemistry, ed. G. Semenza and R. Jacnicke,
pp. 101-76. Amsterdam: Elsevier Science Publishers.
1991
Fifty years of biological research from oxidative phosphorylation
to energy-requiring transport regulation. Annul Rev. Biochem. 60:1.
With D. B. Ullrey. Search for cellular phosphorylation products of
D-allose. Proc. Natl. Acad. Sci. U.S.A. 88:1504.
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Representative terms from entire chapter:
moritz kalckar
