Purification and Calcium Dependence of Transglutaminases from Sheep Hair Follicles | Zendy

Yoshiyuki Kumazawa | Zendy; Tomoko Ohtsuka | Zendy; Daiki Ninomiya | Zendy; Katsuya Seguro | Zendy

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Purification and Calcium Dependence of Transglutaminases from Sheep Hair Follicles

Author(s) -

Yoshiyuki Kumazawa,

Tomoko Ohtsuka,

Daiki Ninomiya,

Katsuya Seguro

Publication year - 1997

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.61.1086

Subject(s) - calcium , chemistry , biology , microbiology and biotechnology , zoology , biochemistry , organic chemistry

To study the calcium sensitivity of sheep hair follicle transglutaminase, which was reportedly calcium-independent [H. W. Harding and G.E. Rogers, Biochemistry, 11, 2858-2863 (1972)], the enzyme was purified from a homogenate of merino sheep hair follicles and its calcium dependence was examined. As a result of purification, two types of transglutaminases (DEAE-unabsorbed and absorbed transglutaminase, DU-TG and DA-TG, respectively) were obtained. The molecular mass of DU-TG was 77 and 82 kDa by SDS-PAGE and gel filtration, respectively, while that of DA-TG was 40 and 80 kDa. Each enzyme was obviously calcium dependent and contained (a) cysteine residue(s) in the active site, like other known mammalian transglutaminases. Maximum activation of DU-TG and DA-TG was observed at 1 and 0.1 mM CaCl2, respectively.

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