Transglutaminase from Hair Follicle of Guinea Pig | Zendy

Soo Im Chung | Zendy; J.E. Folk | Zendy

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Transglutaminase from Hair Follicle of Guinea Pig

Author(s) -

Soo Im Chung,

J.E. Folk

Publication year - 1972

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.69.2.303

Subject(s) - tissue transglutaminase , hair follicle , guinea pig , biochemistry , lysine , polyacrylamide gel electrophoresis , enzyme , follicle , size exclusion chromatography , chemistry , gel electrophoresis , fibrin , biology , microbiology and biotechnology , endocrinology , amino acid , immunology

Two transglutaminases are found in homogenates of the inner root sheaths of guinea pig hair-follicles. One is indistinguishable from the well-characterized liver transglutaminase [J. Biol. Chem. , 246, 1093 (1971)]. The other, which is present in far greater quantity, has not been detected in other organs or tissues. Gel filtration and polyacrylamide gel electrophoresis studies indicate that the native hair-follicle enzyme, of molecular weight 54,000, is composed of two subunits of identical molecular weight. Specificity studies suggest that the intermolecular cross-linking of fibrin and fibrinogen that is catalyzed by this enzyme is a result of the formation of ε(γ-glutamyl)lysine bonds. The probable participation of hair-follicle transglutaminase in the formation of these cross-links in the proteins of hair is discussed.

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