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Transglutaminase in the rat lung is tightly associated with the insoluble matrix which is not extractable with detergent, 0.5 M NaCl, and 40% glycerol solutions. The insoluble matrix was found to be rich in heparin sulfate and poor in collagen, elastin, and DNA. The lung transglutaminase was found to be distinct from tissue transglutaminase (identifiable(More)
The possible role of polyamines in the covalent modification of proteins in CHO cells was investigated by metabolic labeling with [3H]putrescine. A single radiolabeled protein band with an apparent relative molecular mass of 18,000 Da was observed by SDS-polyacrylamide gel electrophoresis. Almost all the radioactivity covalently linked to this protein was(More)
The major form of cross-link found in apolipoprotein B was identified as N1N12-bis-(gamma-glutamyl)spermine, a product known to be formed through the catalytic action of transglutaminases (EC 2.3.2.13). N1-(gamma-Glutamyl)spermine was present in a trace amount but epsilon-(gamma-glutamyl)lysine cross-links, which are formed during fibrin formation in(More)
Multiple molecular forms of transglutaminase are found in cells and each form is widely distributed. We find a 95 K dalton enzyme associated with membrane fractions. A 50 K dalton enzyme occurs primarily in epidermis and hair follicles. Cells after treatment with proteases show greater transglutaminase activity. The activated enzyme in rat chondrosarcoma(More)
Transglutaminases (E.C. 2.3.2.13) are calcium-dependent enzymes that catalyze the covalent cross-linking of proteins, and occur in multiple molecular forms in a variety of tissues. Distribution of each form of transglutaminase varies with different tissues. Studies were undertaken to characterize the form of transglutaminase expressed in rat parotid gland,(More)
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