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CORRELATION BETWEEN VARIOUS PROTEINS OF BOVINE SNOUT EPIDERMIS *
Author(s) -
CARRUTHERS CHRISTOPHER,
BHATTACHARAYA MALAYA
Publication year - 1972
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1972.tb16102.x
Subject(s) - snout , library science , art history , history , medicine , anatomy , computer science
Summary.— A comparison is made of several properties of urea‐extractable proteins which were isolated from mammalian epidermis. A 6 mol/l urea solution extracts from epidermis at least 3 proteins which are precipitated maximally at pH 6·3, 5·5 and 4·5. The urea 4·5 and 5·5 proteins are soluble in water at pH 7·5 to 8·5. The urea 6·3 proteins were rather insoluble in the absence of urea, but were partially solubilized by 0·05 N NaOH to yield protein which precipitated maximally at pH 5·5, the alkali‐soluble 5·5 protein. Also, the —S—S— bonds of the urea 6·3 proteins were reduced with Clelands reagent (dithiothreitol) and the resultant free‐SH groups were reacted with iodoacetate to yield soluble‐ and insoluble‐ S ‐carboxymethyl derivatives of these proteins. The urea 6·3 and alkali‐soluble 5·5 proteins have molecular weights exceeding 20 × 10 6 , whereas the S ‐carboxymethyl proteins have a molecular weight of 2·2 × 10 5 . The urea 5·5 protein extracted from epidermis at room temperature, and a portion of the urea 5·5 protein extracted at 0°C, have a molecular weight of 5·0 × 10 4 . With antisera prepared in rabbits against the urea 5·5 and 6·3 proteins, the following proteins were found to have common antigenic determinants: urea 4·5, 5·5 and 6·3 proteins, alkali‐soluble 5·5 protein, and the S ‐carboxymethyl‐soluble proteins.