نتایج جستجو برای: aspartic acid

تعداد نتایج: 748175  

Journal: :The Journal of biological chemistry 1951
C B ANFINSEN D STEINBERG

Linderstrplm-Lang and Ottesen have reported the discovery of a bacterial enzyme which brings about the transformation of ovalbumin to a new, easily crystallizable protein, plakalbumin. Unlike other proteolytic processes, this reaction seems to involve the rupture of a limited number of peptide bonds, with the release of only slightly over 1 per cent of the total ovalbumin nitrogen (1, 2). Ville...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1974
J L Bada R A Schroeder R Protsch R Berger

By determining the extent of racemization of aspartic acid in a well-dated bone, it is possible to calculate the in situ first-order rate constant for the interconversion of the L and D enantiomers of aspartic acid. Collagen-based radiocarbon-dated bones are shown to be suitable samples for use in "calibrating" the racemization reaction. Once the aspartic-acid racemization reaction has been "ca...

Journal: :Polish journal of microbiology 2007
Mirosław Papierz Grazyna Gadomska Bogusław Sobierajski Aleksander Chmiel

The strain of Escherichia coli K-12 with high aspartase activity was irradiated with UV. After mutagenesis and selection, the mutant B-715 was isolated which was 4-times more active in L-aspartic acid biosynthesis than parental K-12 strain. The highest productivity was achieved while the strain was cultivated in the ammonium fumarate medium in 37 degrees C for 18-30 hours. It was found that bet...

2001
Tomohiro Hiraishi Kenji Tabata Yoshiharu Doi

The microbial and enzymatic hydrolysis of poly(aspartic acid) (PAA) has been reviewed. Two PAA-degrading bacteria (Pedobacter sp. KP-2 and Sphingomonas sp. KT-1) were isolated from flesh river water. Pedobacter sp. KP-2 hydrolyzed PAA of high molecular weights over 5000. Sphingomonas sp. KT-1 hydrolyzed only PAA of low molecular weights (<5000), while the cell extract could hydrolyze high-molec...

Journal: :Journal of Biological Chemistry 2007

Journal: :Journal of the agricultural chemical society of Japan 1964

Journal: :The Journal of antibiotics 1976
J Shoji H Hinoo Y Wakisaka K Koixumi M Mayama

A new peptide antibiotic complex B-43, active against Gram-positive and Gram-negative bacteria, was isolated from a strain of Bacillus circulans. This antibiotic contains aspartic acid, valine, isoleucine, leucine, phenylalanine and 2,4-diaminobutyric acid. It seems to be related to polypeptin and antibiotic complex 4205, but differs in that it contains aspartic acid residue.

Journal: :The Journal of biological chemistry 1991
P Friis C E Olsen B L Møller

Toxin production in a large number of Pyrenophora teres isolates have been investigated. During fungal growth, the pH of the medium decreases from 6.5 to about 3.0. Aspergillomarasmine A is the major toxin excreted into the culture medium. Nonenzymatic acid-catalyzed conversion of aspergillomarasmine A to anhydroaspergillomarasmine A proceeds at low pH and is prevented by repeated titration of ...

Journal: :The Journal of biological chemistry 1949
S RATNER A PAPPAS

A preceding paper described the characteristics of the isolated enzyme system, prepared from ox liver acetone powder, which catalyzes the conversion of citrulline and aspartic acid to arginine and malic acid. It was shown that the fundamental requirements for arginine synthesis from citrulline are aspartic acid, Mg++, and adenosine triphosphate (ATP), the latter as a reactant in substrate conce...

Journal: :Journal of bacteriology 2010
Cristina L Marolda Bo Li Michael Lung Mei Yang Anna Hanuszkiewicz Amanda Roa Rosales Miguel A Valvano

Wzx belongs to a family of membrane proteins involved in the translocation of isoprenoid lipid-linked glycans, which is loosely related to members of the major facilitator superfamily. Despite Wzx homologs performing a conserved function, it has been difficult to pinpoint specific motifs of functional significance in their amino acid sequences. Here, we elucidate the topology of the Escherichia...

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