MU Digital Repository
Logo

Isolation and characterization of a specific enterokinase inhibitor from kidney bean (Phaseolus vulgaris)

Bhat, Gopalakrishna P and Jacob, RT and Pattabiraman, TN (1983) Isolation and characterization of a specific enterokinase inhibitor from kidney bean (Phaseolus vulgaris). Biochem J., 209 (1). pp. 91-97.

[img] PDF
BJ1983.pdf - Published Version
Restricted to Registered users only

Download (1MB) | Request a copy

Abstract

A specific enterokinase inhibitor from kidney bean (Phaseolus vulgaris) was purified to homogeneity. It showed a single protein band on sodium dodecyl sulphate/polyacryl-amide-gel electrophoresis in the presence of mercaptoethanol, and the Mr was 31000. Aspartic acid was identified as the N-terminus of the inhibitor. The Mr by gel chromatography on Sephadex G-200 was found to be 60000, indicating the dimeric nature of the inhibitor. The inhibitor was found to be a glycoprotein. The monosaccharide moieties were glucose, mannose, glucuronic acid and glucosamine in the proportions 3.15%, 5.0%, 0.85% and 1.3% respectively. The inhibitor was most active on pig enterokinase, followed by bovine and human enterokinases. Maximal inhibitory activity was elicited by preincubation of the inhibitor with the enzyme for 15 min. Digestion with pepsin resulted in loss of inhibitory activity. The inhibitor was stable to exposure to a wide range of pH values (2-10), and exposure to pH above 10 resulted in loss of inhibitory activity. Modification of arginine residues by cyclohexane 1,2-dione and ninhydrin led to complete loss of enterokinase-inhibitory activity.

Item Type: Article
Subjects: Medicine > KMC Manipal > Biochemistry
Depositing User: KMC Manipal
Date Deposited: 12 Dec 2011 04:54
Last Modified: 12 Dec 2011 04:54
URI: http://eprints.manipal.edu/id/eprint/1790

Actions (login required)

View Item View Item