Partial purification and characterization of cysteine proteinase inhibitor from chicken plasma.

Abstract

A high-molecular-weight cysteine proteinase inhibitor (CPI) was purified from chicken (Gallus gallus) plasma using polyethylene glycol (PEG) fractionation and affinity chromatography on carboxymethyl-papain-Sepharose-4B. The CPI was purified 96.8-fold with a yield of 28.9%. Based on inhibitory activity staining for papain, CPI was shown to have an apparent molecular mass of 122 kDa. No inhibitory activity was obtained under reducing condition, indicating that CPI from chicken plasma was stabilized by disulfide bonds. CPI was stable in temperature ranges from 40 to 70 degrees C for 10 min; however, more than 50% of the inhibitory activity towards papain was lost within 30 min of heating at 90 degrees C. CPI was stable in the presence of salt up to 3%. The purified CPI exhibited the inhibitory activity toward autolysis of arrowtooth flounder (Atheresthes stomias) and Pacific whiting (Merluccius productus) natural actomyosin (NAM) in a concentration-dependent manner.

• Authors: Saroat Rawdkuen, Soottawat Benjakul, Wonnop Visessanguan, Tyre C Lanier
• Journal: Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (Comp Biochem Physiol B Biochem Mol Biol) Vol. 144 Issue 4 Pg. 544-52 (Aug 2006) ISSN: 1096-4959 [Print] England
• PMID: 16815719 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Blood Proteins
• Cysteine Proteinase Inhibitors
• Actomyosin

Topics

• Actomyosin (chemistry)
• Animals
• Blood Proteins (chemistry, isolation & purification)
• Chickens
• Chromatography, Affinity
• Cysteine Proteinase Inhibitors (chemistry, isolation & purification)
• Fishes
• Muscles (chemistry)