作者: Howard P. Baden , Lowell A. Goldsmith , Barbara Fleming
DOI: 10.1016/0005-2795(73)90225-0
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摘要: Abstract An α-fibrous protein, prekeratin, has been isolated from cow snout epidermis with citrate buffer, pH 2.65. Using acrylamide electrophoresis 0.1% sodium dodecyl sulfate, prekeratin can be shown to contain three polypeptide chains of different molecular weights. The two faster migrating components are very similar a mol. wt about 47 000 while the slower one 58 000. Chromatography on number sieve and exchange resins does not separate components, but use Sepharose 2B 0.1 M Tris, 9.0, containing 10% propanol gives peaks protein. first major peak contains all second only mobility. more rapidly were by electrophoresis, latter an amino acid composition compatible non-helical Enzymatic digestion tosyl- l -phenylalanine chloromethylketone-treated (TPCK-)trypsin shows that component is susceptible hydrolysis than other two. These data suggest homogenous in consists several interacting chains. One these would appear structure.