Detection and assay of proteases using calf lens beta-crystallin aggregateas substrate

Citation
Vd. Trivedi et al., Detection and assay of proteases using calf lens beta-crystallin aggregateas substrate, J BIOCH BIO, 40(1-2), 1999, pp. 49-55
Citations number
11
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS
ISSN journal
0165022X → ACNP
Volume
40
Issue
1-2
Year of publication
1999
Pages
49 - 55
Database
ISI
SICI code
0165-022X(19990728)40:1-2<49:DAAOPU>2.0.ZU;2-Y
Abstract
The eye lens protein, beta(L)-crystallin, aggregates and yields a turbid so lution upon refolding from its denatured state. We have observed that the a ddition of trace amounts of protease results in clearing of this turbidity. Based on this observation, we have developed a simple and rapid method for the detection and assay of proteases. This assay can be performed in the p H range of 6.0-9.0. We could assay the activity of trypsin at a concentrati on as low as 5 mu g/ml. (C) 1999 Elsevier Science B.V. All rights reserved.