Guinea pig liver transglutaminase: A modified purification procedure affording enzyme with superior activity in greater yield

Citation
A. Leblanc et al., Guinea pig liver transglutaminase: A modified purification procedure affording enzyme with superior activity in greater yield, PROT EX PUR, 17(1), 1999, pp. 89-95
Citations number
22
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN EXPRESSION AND PURIFICATION
ISSN journal
10465928 → ACNP
Volume
17
Issue
1
Year of publication
1999
Pages
89 - 95
Database
ISI
SICI code
1046-5928(199910)17:1<89:GPLTAM>2.0.ZU;2-7
Abstract
Tissue transglutaminase purified from guinea pig livers has a very broad su bstrate specificity in comparison with other members of the transglutaminas e family and therefore is useful for substrate analogue kinetic studies. Mo difications made in our laboratory to the standard purification protocol (J . E. Folk and S. I. Chung, 1985, Methods Enzymol. 113, 358-364) have yielde d a 28% increase in specific activity and 55% increase in overall yield, wh ile reducing the number of steps to the purification. Herein we report some of the highest yields and specific activities for guinea pig liver transgl utaminase found in the literature, as well as the use of lyophilization as a solution to the longstanding problem of enzyme stability during storage. (C) 1999 Academic Press.