Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin.

Abstract:

:1. Susceptibility to inhibitors of neutral protease from calf thymus chromatin has been compared with that of trypsin. The chromatin protease reacts stoichiometrically with the inhibitors specific for trypsin (diisopropylfluorophosphate, tosyl-lysyl chloromethane, soybean trypsin inhibitor and Kunitz basic inhibitor from pancreas), but not with the inhibitor specific for chymotrypsin (tosyl-phenylalanyl chloromethane). 2. Chromatin protease, similarly as trypsin, cleaves Lys-X and Arg-X peptide bonds. 3. It is concluded that the structure of active site region of both enzymes is very similar.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Kowalska-Loth B,Zieleński J,Toczko K,Chmielewska I

subject

Has Abstract

pub_date

1976-01-01 00:00:00

pages

139-44

issue

2-3

eissn

0001-527X

issn

1734-154X

journal_volume

23

pub_type

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