title: Primary structure of protamine from the Northern pike Esox lucius.
abstract: The basic nuclear protein in the sperm of the Northern pike is a protamine, 32-residues long, which behaved as a single component during ion-exchange chromatography and gel electrophoresis. Amino acid analysis gave close to molar ratios for the eight different residues with no evidence of microheterogeneity. However, the presence of sequence variants was revealed following a combination of automated protein sequencing and cleavage of the protamine by CNBr, endoproteinase Lys-C and thermolysin. At position 28 there is an equal probability of having serine or glycine. At position 9 glycine is found more frequently than serine. The reciprocal nature of the substitutions results in glycine and serine contents which are close to a 4:2 ratio. Pike protamines are homologous to those of the trout but show less sequence variation between components.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002852:Chromatography, Ion Exchange; D005399:Fishes; D008297:Male; D011479:Protamines / Q000302:isolation & purification*; D013045:Species Specificity; D013094:Spermatozoa / Q000032:analysis; D014337:Trout
chemical_list: D000596:Amino Acids; D011479:Protamines