ISSN:
1573-4943
Keywords:
Cytosolic creatine kinase (rabbit muscle)
;
mitochondrial creatine kinase (pig heart)
;
electrospray ionization mass spectroscopy
;
Edman degradation
;
proteinase K specificity
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Proteinase K cleaves selectively both cytosolic and mitochondrial isoforms of creatine kinase leading to the appearance of two fragments, a large N-terminal one (K1) and a small C-terminal peptide (K2) which remain associated together. The loss of enzymatic activity correlates with the extent of monomer cleavage. N-terminal sequencing of the K2 fragments from rabbit cytosolic and pig mitochondrial creatine kinase shows that these peptides begin with A328 and A324, respectively. Electrospray ionization mass spectrometry demonstrates that K2 peptide is composed of 53 residues (A328–K380). However, the C-terminal end of the K1 fragment is not A327 as expected, but D325. Thus, the amino acids residues T326 and A327 have been eliminated by the protease.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1026347129083
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