Disulfide bonds and free SH-group in pig kidney aminopeptidase P

Biological Chemistry

Volumn 377, Issue 12, 1996, Pages 857-858

  Mann, Karlheinz ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Aminopeptidase P; Disulfide bonds

Indexed keywords

AMINOPEPTIDASE P; CYSTEINE; DISULFIDE; KIDNEY ENZYME;

ANIMAL TISSUE; ARTICLE; DISULFIDE BOND; ENZYME DENATURATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL;

AMINOPEPTIDASES; ANIMALS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DISULFIDES; KIDNEY; SWINE;

EID: 0030444179     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (4)

1. Barzan, J.F., Weaver, L.H., Roderick, S.L., Huber, H., and Matthews, B.W. (1994). Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc. Natl. Acad. Sci. USA 91, 2473-2477.
2. Denslow, N.D., Ryan, J.W., and Nguyen, H.P. (1994). Guinea pig membrane-bound aminopeptidase P is a member of the proline peptidase family. Biochem. Biophys. Res. Commun. 205, 1790-1795.
3. Vergas Romero, C., Neudorfer, I., Mann, K., and Schäfer, W. (1995). Purification and amino acid sequence of aminopeptidase P from pig kidney. Eur. J. Biochem. 229, 262-269.
4. Yaron, A., and Naider, F. (1993). Praline-dependent structural and biological properties of peptides and proteins. Crit. Rev. Biochem. Mol. Biol. 28, 31-81.