Abstract:
:Ultraviolet irradiation of calmodulin in the presence of calcium results in either the intramolecular cross-linking of Tyr99 and Tyr138 [Malencik, D.A., & Anderson, S.R. (1986) Biochemistry 25, 709] or, when [Tyr8]substance P is bound, the generation of peptide-calmodulin adducts. The latter consist of two chromatographically distinct fractions, one of which was purified to homogeneity with phenylagarose, DEAE-Sepharose, and reverse-phase chromatography. Chemical characterization shows that the purified conjugate contains 1 mol/mol of peptide covalently attached to Tyr138 of calmodulin. The fluorescence intensity and anisotropy of the dityrosine moiety demonstrate that this novel derivative undergoes interactions with calcium, smooth muscle myosin light chain kinase, and phenylagarose which are similar to those of unmodified calmodulin.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Malencik DA,Anderson SRdoi
10.1021/bi00403a016subject
Has Abstractpub_date
1988-02-09 00:00:00pages
944-50issue
3eissn
0006-2960issn
1520-4995journal_volume
27pub_type
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