[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.
D000595:Amino Acid Sequence; D000818:Animals; D001797:Blood Protein Electrophoresis; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens / Q000097:blood*; D005260:Female; D006824:Hybridization, Genetic; D007178:Inbreeding; D007525:Isoelectric Focusing; D008297:Male; D008970:Molecular Weight; D012709:Serum Albumin; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet; D013057:Spectrum Analysis
D012709:Serum Albumin
Issledevanie fiziko-khimicheskikh svoĭstv i chastichnoĭ N-kontsevoĭ aminokislotnoĭ posledovatel'nosti syvorotochnogo al'bumina kur