Experientia. Basel 1986-02-15

A thiol protease of peritoneal macrophages in the guinea pig.

T Kambara, S Uchida, J Tanaka, S Shoji

Index: Experientia 42(2) , 155-7, (1986)

Full Text: HTML

Abstract

Proteolytic enzymes of the guinea pig peritoneal exudate macrophages were investigated using synthetic fluorogenic peptide substrates. Among several enzymes, t-butyloxycarbonyl-phenylalanyl-seryl-arginine 4-methylcoumaryl-7-amide cleaving enzymes had the highest activity, and the activity in exudate macrophages was about 3 times stronger than that in resident macrophages. The molecular weight of the enzyme was around 35,000 and optimal pH around 6.5-7.0. It was inhibited by thiol-blocking reagents, suggesting a thiol protease.

Related Compounds

  • Boc-Phe-Ser-Arg-...

Related Articles:

Purification, characterization, and localization of a novel trypsin-like protease found in the human airway.

1997-03-01

[Am. J. Respir. Cell. Mol. Biol. 16(3) , 300-8, (1997)]

Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence.

2010-01-01

[J. Biol. Chem. 270(40) , 23619-26, (1995)]

Detection and characterization of endogenous protease associated with desquamation of stratum corneum.

1993-01-01

[Arch. Dermatol. Res. 285(6) , 372-7, (1993)]

pH dependence of bovine mast cell tryptase catalytic activity and of its inhibition by 4',6-diamidino-2-phenylindole.

1997-05-12

[FEBS Lett. 408(1) , 85-8, (1997)]

Purification and characterization of novel trypsin-like serine proteases from mouse spleen.

1996-04-01

[J. Biochem. 119(4) , 633-8, (1996)]

More Articles...