title: Guinea pig liver transglutaminase: A modified purification procedure affording enzyme with superior activity in greater yield.
abstract: Tissue transglutaminase purified from guinea pig livers has a very broad substrate specificity in comparison with other members of the transglutaminase family and therefore is useful for substrate analogue kinetic studies. Modifications made in our laboratory to the standard purification protocol (J. E. Folk and S. I. Chung, 1985, Methods Enzymol. 113, 358-364) have yielded a 28% increase in specific activity and 55% increase in overall yield, while reducing the number of steps to the purification. Herein we report some of the highest yields and specific activities for guinea pig liver transglutaminase found in the literature, as well as the use of lyophilization as a solution to the long-standing problem of enzyme stability during storage.
authors.affiliation: Département de Chimie, Université de Montréal, Montréal, Québec, Canada H3C 3J7.
authors.forename: A
authors.initials: A
authors.lastname: Leblanc
authors.forename: N
authors.initials: N
authors.lastname: Day
authors.forename: A
authors.initials: A
authors.lastname: Ménard
authors.forename: J W
authors.initials: JW
authors.lastname: Keillor
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005612:Freeze Drying; D006168:Guinea Pigs; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity; D011503:Transglutaminases / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D011503:Transglutaminases