Chymotrypsin c

Department of Biochemistry, Eotvos Lorand University, and 2Biotechnology Research Group of the Hungarian Academy of Sciences, ´ ´ ´ ´ Pazmany setany 1/C, Budapest, Hungary The molecular mechanism of the autolysis of rat a-chymotrypsin B was investigated. In addition to the two already known autolytic sites, Tyr146 and Asn147, a new site formed by Phe114 was identified. The former two sites and the latter one are located in the autolysis and the interdomain loops, respectivel

9p system191 01-06-2013 39 4   Download

Bovineb-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65°C at neutral pH. At these temperaturesb-lactoglobulin undergoes signi®cant but reversible structural changes. In the conditions used in the present study,b-lactoglobulinwas virtually insensitive to proteolysis by either enzyme at room temperature, but underwent extensive proteolysis when either proteasewas present during the heat treatment.

11p research12 29-04-2013 33 3   Download

The 3C-like protease of the severe acute respiratory syndrome (SARS) cor-onavirus has a C-terminal extra domain in addition to the chymotrypsin-fold adopted by piconavirus 3C proteases hosting the complete catalytic machinery. Previously we identified the extra domain to be involved in enzyme dimerization which has been considered essential for the catalytic activity.

11p inspiron33 26-03-2013 41 4   Download

Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation. Mutations that abolish activity or secretion of CTRC increase the risk for chronic pancreatitis.

13p cosis54 09-12-2012 40 2   Download