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Showing papers in "Journal of Biological Chemistry in 1962"


Journal Article•DOI•
Stanley Cohen1•
TL;DR: The isolation of the factor responsible for the earlier development of the incisors and eyelids is reported here, a heat-stable, nondialysable, antigenic protein, whose most distinctive chemical characteristic is the absence of phenylalanine and lysine.

2,109 citations


Journal Article•DOI•
TL;DR: Data indicated a significant role for the enzyme in the control of the levels of adenosine 3’,5’-phosphate present in biological systems, which was very desirable because of the extremely low levels present in most biological materials.

2,056 citations



Journal Article•DOI•
TL;DR: Evidence is presented which suggests that this enzyme participates in a microsomal elect,ron transport system which does not include cytochrome c and kinetic evidence has been obtained which allows certain conclusions to be drawn concerning the mechanism of catalysis by this enzyme.

1,378 citations


Journal Article•DOI•
TL;DR: A feedback inhibition is investigated to learn more about its enzymological mechanism and it is shown that in the bacterium the activity of aspartate transcarbamylase is closely controlled by an end product, probably a cytosine de- rivative, and that inhibition of this enzyme is important for controlling the whole pathway.

924 citations


Journal Article•DOI•
Charles Williams1, Henry Kamin1•
TL;DR: The biological role of reduced triphosphopyridine nucleotide (TPNH) and the metabolic pathways of its hydrogen atom and electron appear to be fundamentally different from those of reduced diphosphipyridineucleotide (DPNH).

889 citations





Journal Article•DOI•
TL;DR: Investigation into the mechanisms by means of which the rate of urea synthesis is altered in response to differences in dietary protein consumption indicate that adaptation to differing consumption of protein involves changes in activities of all urea cycle enzymes in the liver.

665 citations


Journal Article•DOI•
TL;DR: This chapter discusses enzymology and its applications in medicine, particularly in the field of regenerative medicine and its role in the treatment of cancer.



Journal Article•DOI•
TL;DR: The assay, purification, properties, and distribution of an enzyme, phenylethanolamine-N-methyl transferase, that N-methylates the nitrogen of norepinephrine as well as that of a number of phenylethaolamine derivatives are described.

Journal Article•DOI•
TL;DR: Bello, Van Bibber, and Bessman have shown that the deoxyguanylate kinase of infected cells is physically distinct and separable from the host cell enzyme, and the polymerase of uninfected E. coli (E. coli polymerase) and the T2 polymerase are distinct and different enzymes.


Journal Article•DOI•
Norman Kirshner1•
TL;DR: Chromaffin granules isolated from beef adrenal medulla took up C(14)-labeled catecholamines from an isotonic medium at 37 degrees C at a rate approximately 20 times the rate at 0 degrees C as discussed by the authors.

Journal Article•DOI•
TL;DR: The mold Polyporus circinatus produces an extracellular oxidase that catalyzes the oxidation of n-galactose, but the enzyme does not possess a flavin prosthetic group, and preliminary evidence suggests that it may be a metalloprotein.


Journal Article•DOI•
TL;DR: The chemical shifts of the proton magnetic resonance spectra in the nucleotides could be compared with the shifts in the metal complexes to determine the interaction of the metal ion with the adenine ring, thus specifying the nature of the met.al complexes formed.





Journal Article•DOI•
TL;DR: Three recent studies suggest that fragmentation of the electron transfer chain by the methods in common use may be carried so far that the function and the structure of the complexes within the system are irreversibly destroyed.


Journal Article•DOI•
TL;DR: The glutamate oxaloacetate enzyme is a mechanistic prototype for a large number of experimentally less accessible transaminases and also for the general class of group-transferring enzymes, which operate exclusively through binary enzyme substrate complexes.