Parvalbumins from coelacanth muscle. I. General survey.
Parvalbumins from coelacanth (Latimeria chalumnae) myogen have been isolated by gel filtration of Sephadex G-75 and DEAE-cellulose chromatography. Disc electrophoresis and cellulose acetate electrophoresis showed the homogeneity of the three first major parvalbumin peaks (pI = 5.44, pI = 4.95 and pI = 4.52). The fourth component was partially resolved into two more parvalbumins (pI = 3.78 and pI = 3.50) by preparative gel electrophoresis. Amino acid analyses and tryptic peptide maps separated the five components in two major categories. The two less acidic components differ only in the presence or absence of an N-terminal blocking group. The three more acidic components constitute the second category; in spite of this heterogeneity, they share the same amino acid sequence.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004589:Electrophoresis, Disc; D005399:Fishes; D008297:Male; D008970:Molecular Weight; D009124:Muscle Proteins; D009132:Muscles; D010320:Parvalbumins; D013053:Spectrophotometry
D000596:Amino Acids; D009124:Muscle Proteins; D010320:Parvalbumins