Enzyme 1987-01-01

Determination and characterization of succinyl tri-alanine p-nitroanilide hydrolyzing metalloendopeptidase in serum.

M Ishida, M Ogawa, T Mori, T Mega

Index: Enzyme 37(4) , 202-7, (1987)

Full Text: HTML

Abstract

Serum succinyl (Ala)3-p-nitroanilide hydrolyzing elastase-like activity which elevates in patients with obstructive jaundice, is due to the joint action of two enzymes: first, succinyl (Ala)3-p-nitroanilide is cleaved to succinyl (Ala)2 and Ala-p-nitroanilide by metalloendopeptidase, and then Ala-p-nitroanilide is cleaved to Ala and p-nitroaniline by aminopeptidase. We adopt a new assay method for serum endopeptidase activity using HPLC.

Related Compounds

  • Suc-Ala-Ala-Ala-...

Related Articles:

A new Kunitz-type plasmin inhibitor from scorpion venom.

2015-11-01

[Toxicon 106 , 7-13, (2015)]

SjAPI, the first functionally characterized Ascaris-type protease inhibitor from animal venoms.

2013-01-01

[PLoS ONE 8(3) , e57529, (2013)]

Purification, kinetical and molecular characterizations of a serine collagenolytic protease from greenshore crag (Carcinus maenas) digestive gland.

1996-09-01

[Comp. Biochem. Physiol. B Biochem. Mol. Biol. 115(1) , 87-95, (1996)]

Characterization of metalloelastase-like activity from the plasma of a patient with Tangier disease.

1991-12-01

[Biol. Chem. Hoppe-Seyler 372 , 1057-1064, (1991)]

Determination of elastase inhibitory activity of alpha 1-proteinase inhibitor and bronchial antileukoprotease: different results using insoluble elastin or synthetic low molecular weight substrates.

1987-06-01

[Scand. J. Clin. Lab. Invest. 47(4) , 405-10, (1987)]

More Articles...