Biomedical subjects

G HAMOIR

Publications and source records attributed to G HAMOIR.

17 recordsLinked to original sources

PubMed1965

CARP MYOGENS OF WHITE AND RED MUSCLES. GENERAL COMPOSITION AND ISOLATION OF LOW-MOLECULAR-WEIGHT COMPONENTS OF ABNORMAL AMINO ACID COMPOSITION.

1. The general composition of the carp myogens of white and red muscles was examined by electrophoresis and ultracentrifugation. 2. Eight and nine peaks were found in the electrophoretic analysis at pH7.3 and I0.075 of white and red muscle respectively. Lowering of the pH to 5 or 6 did not increase the number of peaks. The electrophoretic pattern of white-muscle myogen was remarkably different from that of red-muscle myogen, though ultracentrifugal analyses of the both types of myogen gave similar diagrams, in which about one-third of the total myogen sedimented slowly. 3. The pH-mobility curves of the myogen of white muscle indicated that the net charges of the components 2, 3 and 5 vary only slightly within the pH range 7.3-5.4, suggesting that their histidine content is very low. 4. The slow-sedimenting fraction of white-muscle myogen was isolated in fairly good yield by ammonium sulphate fractionation, by taking advantage of their high salting-out range, and the fraction was shown to be composed mainly of components 2, 3 and 5. 5. The same method of fractionation was applied to red-muscle myogen and the absence of the three components was confirmed. These results bring to light a new difference between the two types of fish muscle.

Amino Acids↗

PubMed1965

CARP MYOGENS OF WHITE AND RED MUSCLES. PROPERTIES AND AMINO ACID COMPOSITION OF THE MAIN LOW-MOLECULAR-WEIGHT COMPONENTS OF WHITE MUSCLE.

1. The three main components of the 1.5-2s ultracentrifugal peak of carp myogen (white muscle) have been isolated by ammonium sulphate fractionation and zone electrophoresis, and crystallized. 2. The molecular weights of these three proteins were determined by sedimentation and diffusion, by the Archibald method and by amino acid analysis, and found to lie between 9000 and 13000. 3. Their complete amino acid compositions were determined by column chromatography and by their ultraviolet spectra. Both methods revealed abnormal compositions, including the absence of tryptophan and methionine and the presence of large amounts of phenylalanine. At most 1 residue each of tyrosine, cysteine, proline, arginine and histidine was found/molecule. 4. The specific viscosity of component 3 was lower than that of other small globular proteins described so far, a fact that suggests that these proteins approximate more closely to the ideal case of the spherical protein molecule. Also, the presence of a single residue of several amino acids, the absence of disulphide bonds, and the apparent reversibility of denaturation by urea of component 3 suggest that the study of these molecules could provide new information on the structure of proteins.

Amino Acids↗

PubMed1965