Mobility of sodium dodecyl sulphate - protein complexes
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چکیده
منابع مشابه
Mobility of sodium dodecyl sulphate - protein complexes.
Reduced and unreduced lysozyme aggregates formed by formaldehyde cross-linking comprise a set of model compounds for studying the effects of protein conformation on the electrophoretic mobilities of sodium dodecyl sulphate-protein complexes. The reduced aggregates were indistinguisable from normal proteins, but the unreduced aggregates migrated anomalously fast by about 14%. Contrary to expecta...
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Polypeptide chain weights of a-, 8and y-gliadin fractions have been estimated by polyacrylamide gel electrophoresis in the presence of mercaptoethanol and sodium dodecyl sulphate. Values lie in the range 32 000 to 44 OOO. When available data on the amino acid analyses were adjusted and compared, significant similarities emerged. It is suggested that these gliadins contain a minimum of 4 cystine...
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The interaction of sodium dodecyl sulfate with a wide variety of proteins is characterized by a high binding ratio when the monomer concentration of amphiphile exceeds 5 x 10W4 M. This binding ratio on a gram to gram basis is identical for all proteins investigated. The protein portion of the complex contains a high degree of order, and hydrodynamic studies suggest that the complex is a rodlike...
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Maltase-glucoamylase (a-D-ghcoside glucohydrolase, EC 3.2.1.20) is a glycoprotein ectoenzyme of the intestinal brush-border membrane. It appears to be the largest component of this membrane (Galand & Forstner, 19746; Maestracci et al., 1975) and its mol.wt. has been estimated by a number of methods to be 4 x 105-5x lo5 (Forstner, 1971 ; Galand & Forstner, 1974~ ; Maestracci et af., 1975). Despi...
متن کاملMolecular-weight estimates of milk-fat-globule-membrane protein-sodium dodecyl sulphate complexes by electrophoresis in gradient acrylamide gels.
The molecular weights of milk-fat-globule-membrane proteins solubilized in sodium dodecyl sulphate were estimated by gradient gel electrophoresis. Standard curves were calibrated from both protein and glycoprotein markers of known molecular weight. Six major proteins were observed with Coomassie Blue staining and six with periodic acid-Schiff staining. The behaviour of the membrane proteins and...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1976
ISSN: 0264-6021
DOI: 10.1042/bj1530191