原著
Phage Proteinに関する研究 (VII)
P22 phage coat protein 3 分画の分子構造 (その1)
1972 年 18 巻 1 号 p. 106-111
詳細
1972 年 18 巻 1 号 p. 106-111
Amino acid analysis, N-terminal determination, reductive cleavage of the S-S bond with mercaptoethanol and the estimation of the molecular weight were carried out with the 3 fractions of P22 phage coat protein. Results obtained were summarized as follows : 1) It was suggested that F1, F2 and F3 differed even in their primary molecular structure. 2) The molecular weight of F1, F2 and F3 were 125,000, 39,000 and 32,000, respectively, so far estimated by the method of Shapiro et al. 3) From the amino acid molar ratio, the molecular weights were caculated as 122,000. for F1 and 25,650 for F3. 4) N-terminal amino acid was valine samely in F1, F2 and F3, irrespective of their difference in immunresponse and presumed molecular structure. 5) After cleavage of the S-S bond by treatment with mercaptoethanol, F1 showed almost same migration as the original F1 molecule, whereas F2 and F3 showed slower migration than originals. This facts show the difference in secondary or tertiary molecular configuration of the three fractions, especially with refference to the intermolecular S-S bonds.
