Purification and characteristics of a novel transglutaminase derived from microorganisms.
Hiroyasu Ando, Masae ADACHI, Koichi Umeda, Akira Matsuura, Masahiko NONAKA, Ryosuke Uchio, Haruo Tanaka, Masao Motoki
Abstract
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Hiroyasu Ando, Masae ADACHI, Koichi Umeda, Akira Matsuura, Masahiko NONAKA, Ryosuke Uchio, Haruo Tanaka, Masao Motoki
Abstract
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A microorganism producing transglutaminase was screened as an indication of hydroxamateform ing activity. The microbial transglutaminase was purified from the culture filtrate of the strain, S-8112, which was supposed to belong to the genus Streptoverticillium. The molecular weight of the purified enzyme was found to be about 40, 000 on SDS-polyacrylamide gel electrophoresis, the isoelectric point 8.9 and the optimal pH of the reaction 6-7. The present enzyme requires no calcium ions for its activity. Thus, it clearly differs from known transglutaminases derived from mammalian organs, which have been defined as calcium-dependent enzymes.
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A microorganism producing transglutaminase was screened as an indication of hydroxamateform ing activity. The microbial transglutaminase was purified from the culture filtrate of the strain, S-8112, which was supposed to belong to the genus Streptoverticillium. The molecular weight of the purified enzyme was found to be about 40, 000 on SDS-polyacrylamide gel electrophoresis, the isoelectric point 8.9 and the optimal pH of the reaction 6-7. The present enzyme requires no calcium ions for its activity. Thus, it clearly differs from known transglutaminases derived from mammalian organs, which have been defined as calcium-dependent enzymes.
Key concepts: Tissue transglutaminase, Isoelectric point, Chemistry, Enzyme, Microorganism, Biochemistry, Polyacrylamide gel electrophoresis, Isoelectric focusing