Amine incorporation into insulin as catalyzed by transglutaminase

Mycek, Mary J.; Clarke, Donald D.; Neidle, Amos; Waelsch, Heinrich

doi:10.1016/0003-9861(59)90613-7

Cited by 114 publications

(34 citation statements)

References 15 publications

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“…Waelsch was immediately fascinated by this process and he studied it in detail, discovering that it was linked to protein crosslinkage as well as to deamidation of glutamine residues in proteins by mechanisms which were reminiscent of those of proteinases (Pincus and Waelsh 1968). Indeed, when insulin was used as a substrate for transglutaminase, it was observed that ammonia was enzymatically released in the absence of amine (Micek et al 1959). The same behavior was observed by Folk and Cole (1965) using synthetic blocked glutamine dipeptides and in the case of many proteolytic enzymes that catalyze both hydrolytic and transpeptidation reactions (Mycek and Fruton 1957).…”

Section: Early Yearssupporting

confidence: 54%

An overview of the first 50 years of transglutaminase research

2008

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Section: Early Yearssupporting

confidence: 54%

An overview of the first 50 years of transglutaminase research

2008

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“…The gels were formed in test tubes of 12 mm diameter by the method just described. Several denaturants (10% SDS, 10% 2-mercaptoethanol, 6.6 M urea and 6 M guanidium hydrochloride solution) were then added to them. After the mixtures had been shaken at 25°C for 10min, the appearance of the gels in each denaturant was observed.…”

Section: Methodsmentioning

confidence: 99%

Gelation Mechanism of Protein Solution by Transglutaminase

Nio

Motoki

Takinami

1986

Agricultural and Biological Chemistry

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“…Work in this laboratory has centered on guinea pig liver transglutaminase, an enzyme that catalyzes formation of -y-glutamyl amide bonds (9,10) by way of an acyl-transfer mechanism (I1). The wide occurrence and obvious importance of y-glutamyl amide bonds has led us to focus attention on the various enzymes responsible for their formation.…”

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confidence: 99%

Transglutaminase from Hair Follicle of Guinea Pig

Chung

Folk

1972

Proc. Natl. Acad. Sci. U.S.A.

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Two transglutaminases are found in homogenates of the inner root sheaths of guinea pig hairfollicles. One is indistinguishable from the well-characterized liver transglutaminase [J. Biol. Chem., 246, 1093]. 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 e(y-glutamyl)lysine bonds. The probable participation of hair-follicle transglutaminase in the formation of these cross-links in the proteins of hair is discussed.The essential role in protein structure of intramolecular covalent crosslinks, in the form of disulfide bonds, has been recognized for many years (ref. 1 for review). There is an increasing awareness of the physiological importance of other covalent crosslinks, within and between protein molecules. Two types of chemical bonds are known to comprise these crosslinks. One, which occurs in collagen and elastin, is the combination of lysine-and hydroxylysine-derived aldehyde condensation products and Shiff bases formed by coupling of these aldehydes with e-amino groups (ref. 2 for review). The second is the e(-y-glutamyl)lysine amide bonds formed during the stabilization of fibrin clot (3-5), and reported to occur in cultures of chicken-breast muscle (6), I-cell membrane (6), native wool keratin (7), and the citrulline-containing protein fraction of hair (8).Work in this laboratory has centered on guinea pig liver transglutaminase, an enzyme that catalyzes formation of -y-glutamyl amide bonds (9, 10) by way of an acyl-transfer mechanism (I1). The wide occurrence and obvious importance of y-glutamyl amide bonds has led us to focus attention on the various enzymes responsible for their formation. Transglutaminases derived from plasma and platelet protransglutaminases (blood coagulation Factor XIII) through thrombin activation (ref. 12 for review) are responsible for the stabilization of fibrin clot, a consequence of formation of e(yglutamyl)lysine bridges between fibrin monomers. Purified transglutaminase from guinea pig liver stabilizes both fibrin (13) and fibrinogen (14) The other, which is present in far greater quantity, is distinctly different from previously described enzymes, and is the principal subject of this paper. MATERIALS AND METHODSSkins from 20-to 25-week-old guinea pigs were obtained packed in dry ice from Rockland (Gilbertsville, Pa. RESULTS Isolation of enzymesStep 1. Hair follicles of the guinea pig were,exposed by the wax-sheet method (17, 18) with a beeswax-rosin mixture at a temperature not exceeding 55°C. The inner-root sheaths were

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Amine incorporation into insulin as catalyzed by transglutaminase

Cited by 114 publications

References 15 publications

An overview of the first 50 years of transglutaminase research

An overview of the first 50 years of transglutaminase research

Gelation Mechanism of Protein Solution by Transglutaminase

Transglutaminase from Hair Follicle of Guinea Pig

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