This paper is only available as a PDF. To read, Please Download here.
Inactivation of transglutaminase by 14C-iodoacetamide is accompanied by a proportional uptake of 14C-carbamidomethyl. Incorporation of 1 mole of this group per mole of enzyme results in complete inactivation. Proteolytic digestion of 14C-carbamidomethyl-labeled enzyme yields two related radioactive peptides containing the S-(14C-carbamidomethyl)cysteinyl residue. The amino acid sequences of these peptides have been determined as Gly-Gln-S-(carbamidomethyl)cysteine-Trp and Tyr-Gly-Gln-S-(carbamidomethyl)cysteine-Trp.
References
- Arch. Biochem. Biophys. 1959; 79: 338
- J. Biol. Chem. 1965; 240: 2951
Folk, J. E., and Cole, P. W., Biochim. Biophys. Acta, in press.
- J. Am. Chem. Soc. 1954; 73: 4331
- J. Biol. Chem. 1962; 237: 2184
- Anal. Chem. 1958; 3: 1190
- Anal. Chem. 1948; 20: 30
- J. Biol. Chem. 1965; 240: 181
- Goodwin T.W. Harris J. Hartley B.S. Structure and activity enzymes. Academic Press, Inc., New York1964: 87
- Goodwin T.W. Harris J.I. Hartl B.S. Structure and activity of enzymes. Academic Press, In New York1964: 97
- Pre Natl. Acad. Sci. U. S. 1964; 52: 1276
- Boyer P.D. Lardy H. Myrbäck K. The enzymes. Ed. 2. Academic Pre Inc., New York1960: 133
Article info
Publication history
Published online: July 10, 1966
Received:
April 7,
1966
Identification
Copyright
© 1966 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
User license
Creative Commons Attribution (CC BY 4.0) | How you can reuse 
Elsevier's open access license policy
Creative Commons Attribution (CC BY 4.0)
Permitted
- Read, print & download
- Redistribute or republish the final article
- Text & data mine
- Translate the article
- Reuse portions or extracts from the article in other works
- Sell or re-use for commercial purposes
Elsevier's open access license policy
