Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Adolph Abrams"'
Publikováno v:
The Journal of biological chemistry. 164
Autor:
Adolph Abrams, Gary W. Zlotnick
Publikováno v:
Archives of Biochemistry and Biophysics. 230:517-524
The soluble ATPase isolated from Streptococcus faecalis membranes containing tightly bound endogenous nucleotides do not exchange in the presence of ATP and Mg+2 added during the purification of the enzyme. In this paper the stoichiometry of endogeno
Publikováno v:
Biochemistry. 15:5560-5566
Publikováno v:
Biochemical and Biophysical Research Communications. 69:804-811
ATPase extracted from Streptococcus faecalis membranes was purified by preparative slab gel electrophoresis in the presence of Mg ++ (plus Mg 2+ ATPase) and without Mg 2+ (minus Mg 2+ ATPase). The subunit composition and membrane binding capacity of
Autor:
Carl Baron, Adolph Abrams
Publikováno v:
Biochemistry. 7:501-507
Autor:
Adolph Abrams, D.G. Brown
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 200:522-537
1. 1.|The existence of both membrane-associated and cytoplasmic ribosomes in Streptococcus fecalis prompted us to investigate whether or not they are identical. Ribosomes were isolated from the cytoplasmic and membrane fractions of Streptococcus feca
Publikováno v:
Experimental Biology and Medicine. 45:46-49
Summary(1) Contrary to Brakefield, and in agreement with Quick, we find that in humans an appreciable quantity of benzoic acid is excreted as the glucuronide. The ingestion of 5, 6, and 7 g of benzoic acid leads to an excretion of some 5% in the form
Publikováno v:
Journal of Biological Chemistry. 244:2261-2268
N,N′-Dicyclohexylcarbodiimide (DCCD) was found to be a potent inhibitor of the membrane-bound ATPase of Streptococcus faecalis but did not inhibit the solubilized form of the enzyme. Inhibited membrane-bound ATPase was reactivated by releasing the
Autor:
Adolph Abrams, L. Nielsen
Publikováno v:
Biochemical and Biophysical Research Communications. 17:680-684
Autor:
Peter McNamara, Adolph Abrams
Publikováno v:
Journal of Biological Chemistry. 237:170-175