[Physico-chemical properties and partial N-terminal amino acid sequence of chicken serum albumin].

Studies have been made on the molecular weight, solubility, electrophoretic mobility, isoelectric point and N-terminal fragments containing 4 amino acids of the serum albumin in two strains of hens and their hybrids. In all the animals studied, the albumin had Asp as the N-terminal amino acid. Amino acid sequence in the 4-acid fragments was also identical: NH2--Asp--Ala--His--Lys. With respect to all the physico-chemical parameters investigated (except isoelectric point), proteins of the parental strains and of their hybrids did not exhibit significant differences.