Purification and partial characterization of an amino acid alpha,beta- dehydrogenase, L-tryptophan 2‘,3‘-oxidase from Chromobacterium violaceum.

The conversion of the reducible divalent cross-links in collagen to non-reducible multivalent cross-links in mature collagen has resulted in the identification of several new amino acids as the putative mature cross-link. None of these compounds has completely satisfied the necessary criteria. We have now isolated an amino acid of high Mr, derived from lysine, that is only present in high-Mr peptides derived from mature collagen. Its increase with age of the tissue correlates with the decrease in the reducible cross-links, and it is present both in mature skin and bone, which are initially cross-linked through the aldimine and oxo-imine divalent cross-link respectively. We propose that this amino acid, as yet incompletely characterized and designated compound M, is a major cross-link of mature collagen.

Download Full-text

Purification and partial characterization of the 7-d-glutamyl-l-di-amino acid endopeptidase ii from bacillus sphaericus

International Journal of Biochemistry ◽

10.1016/0020-711x(92)90041-x ◽

1992 ◽

Vol 24 (3) ◽

pp. 471-476 ◽

Cited By ~ 11

Author(s):

Thierry Bourgogne ◽

Marie-Jeanne Vacheron ◽

Micheline Guinand ◽

Georges Michel

Keyword(s):

Amino Acid ◽

Bacillus Sphaericus ◽

Partial Characterization

Download Full-text

Identification and Partial Characterization of a Novel CYP2C9 Splicing Variant Encoding a Protein Lacking Eight Amino Acid Residues

Drug Metabolism and Pharmacokinetics ◽

10.2133/dmpk.22.187 ◽

2007 ◽

Vol 22 (3) ◽

pp. 187-194 ◽

Cited By ~ 5

Author(s):

Noritaka Ariyoshi ◽

Yoko Shimizu ◽

Yukari Kobayashi ◽

Hiroyoshi Nakamura ◽

Hiromitsu Nakasa ◽

...

Keyword(s):

Amino Acid ◽

Partial Characterization ◽

Amino Acid Residues ◽

Splicing Variant

Download Full-text

Purification, N-Terminal Amino Acid Sequence and Partial Characterization of A Cu,Zn Superoxide Dismutase From the Pathogenic FungusAspergillusfumiga Tus

Free Radical Research ◽

10.3109/10715769509150324 ◽

1995 ◽

Vol 22 (6) ◽

pp. 519-531 ◽

Cited By ~ 29

Author(s):

M. D. Holdom ◽

R. J. Hay ◽

A. J. Hamilton

Keyword(s):

Superoxide Dismutase ◽

Amino Acid ◽

Amino Acid Sequence ◽

Partial Characterization ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Terminal Amino Acid Sequence

Download Full-text

Purification and partial characterization of the exotoxin of Corynebacterium ovis

Biochemical Journal ◽

10.1042/bj1770181 ◽

1979 ◽

Vol 177 (1) ◽

pp. 181-186 ◽

Cited By ~ 8

Author(s):

E O Onon

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Phospholipase D ◽

Partial Characterization ◽

Assay Method ◽

Nomenclature Committee ◽

Erythrocyte Lysis

1. The toxin from Corynebacterium ovis, a phospholipase D (sphingomyelin phosphodiesterase D) that acts on 2-lysophosphatidylcholine and sphingomyelins, was purified by about 400-fold to homogeneity as judged by several criteria. [The EC number of the toxin (EC 3.1.4.41) has been allotted by the Nomenclature Committee of IUB, but has not yet been published.] 2. A new assay method performed in vitro, based on inhibition by the toxin of erythrocyte lysis by staphylococcal beta-haemolysin, was developed to facilitate the purification. 3. The toxin was found to be a basic (pI9.1) glycoprotein of mol.wt. 14,500 +/- 1,000. 4. The amino acid composition of the toxin was highly reminiscent of that of collagen, since it contained hydroxyproline, hydroxylysine and a high proportion of glycine, but preliminary tests showed no other similarities to collagen or proteins with similar compositions.

Download Full-text