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. 1972 Feb;69(2):303–307. doi: 10.1073/pnas.69.2.303

Transglutaminase from Hair Follicle of Guinea Pig

S I Chung 1, J E Folk 1
PMCID: PMC426445  PMID: 4501114

Abstract

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.

Keywords: crosslinking, fibrin, glutamyllysine, isoenzymes, purified enzyme

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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