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The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes






Biochemical Journal 143(1): 171-179

The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes

The major (14)C-labelled peptides from creatine kinase from normal and dystrophic chicken muscle obtained by carboxymethylating the reactive thiol groups with iodo[2-(14)C]acetic acid and digestion with trypsin were purified by ion-exchange chromatography on Dowex-50 (X2) and by paper electrophoresis. The chromatographic characteristics of the (14)C-labelled peptides, their electrophoretic mobilities at pH6.5, and their amino acid compositions were identical for the two enzymes. The sequence of amino acids around the essential thiol groups of creatine kinase from normal and dystrophic chicken muscle was shown to be Ile-Leu-Thr-CmCys-Pro-Ser-Asn-Leu-Gly-Thr-Gly-Leu-Arg (CmCys, carboxymethylcysteine). This sequence is almost identical with that for the creatine kinases in human and ox muscle and bovine brain and is very similar to that of arginine kinase from lobster muscle. Antibodies to the enzymes were raised in rabbits and their reaction with the creatine kinase from normal and dystrophic muscles in interfacial, immunodiffusion and immunoelectrophoretic experiments was studied. The cross-reaction between normal muscle creatine kinase and antisera against the dystrophic muscle enzyme (or vice versa) observed by immunodiffusion and by immunoelectrophoretic experiments further suggests that the enzymes from normal and dystrophic chicken muscle are similar in structure. The results of the present study, the identical amino acid sequence of the peptides containing the reactive thiol group from both the normal and dystrophic chicken muscle enzymes and the immunological similarities of the two enzymes are in accord with the similarity of the two enzymes observed by Roy et al. (1970).


Accession: 006599385

PMID: 4219281

DOI: 10.1042/bj1430171



Related references

Roy, B.P.; Laws, J.F.; Thomson, A.R., 1970: Preparation and properties of creatine kinase from the breast muscle of normal and dystrophic chicken (Gallus domesticus). 1. The purification of creatine kinase from normal and genetically dystrophic chicken breast muscle is described. Enzyme recovery was significantly lower from dystrophic muscle. 2. Both enzymes had the same number of reactive and total thiol group...

Simpson, I.A.; Hollaway, M.R.; Beard, J., 1977: The subunit structure of rabbit skeletal muscle phospho fructo kinase ec 2.7.1.11 and the amino acid sequence of the tryptic peptide containing the highly reactive thiol group. The single highly reactive (class I) thiol group/80,000-MW subunit of skeletal muscle phosphofructokinase [EC 2.7.1.11] was specifically carboxymethylated with iodo[2-14C]acetate, and after denaturation the remaining thiol groups were carboxymethy...

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Bennett, V.D.; Hall, N.; DeLuca, M.; Suelter, C.H., 1985: Decreased mitochondrial creatine kinase activity in dystrophic chicken breast muscle alters creatine-linked respiratory coupling. Dystrophic chicken breast muscle mitochondria contain significantly less mitochondrial creatine kinase than normal breast muscle mitochondria. Breast muscle mitochondria from normal 16- to 40-day-old chickens contain approximately 80 units of mito...

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Roy, B.; Laws, J.; Thomson, A., 1970: Preparation and properties of creative kinase from the breast muscle of normal and dystrophic chicken (Gallus domesticus). Bio chemical journal: 120 (1) 177-185

Husic H.D.; Suelter C.H., 1980: The rates of disappearance of chicken breast muscle amp amino hydrolase and pyruvate kinase from the plasma of normal and genetically dystrophic chickens. Federation Proceedings 39(6): ABSTRACT 2982

Atherton, R.S.; Laws, J.F.; Miles, B.J.; Thomson, A.R., 1970: Brain 5 atp creatine phospho transferase ec 2.7.3.2 purification thiol group reactivity and the amino acid sequence around the reactive thiol groups. Biochemical Journal 120(3): 589-600

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