ENZYMATIC TREATMENT AND DYE BINDING ABILITY OF SERUM ALBUMIN
- 1 March 1955
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 42 (2) , 111-122
- https://doi.org/10.1093/oxfordjournals.jbchem.a126513
Abstract
Proteolytic hydrolysis of crystalline bovine serum albumin was studied spectrophotometrically with the use of methyl orange (cf. Shimao, K., Jour. Biochem. (Tokyo). 39, 241(1952)) as well as by non-protein N of the deproteinized filtrate with 0.15[image] CCl3COOH. Approximately equal hydrolytic rates by determination with the dye-binding method (RD) and the NPN one (RN) were obtained with hydrolysis by pepsin (pH 3.8 and 4.3), by papain (pH 5.5), and by trypsin (pH 6.4); during hydrolysis by pepsin (pH 5.5 and 6.4) and by trypsin (pH 6.3), RD was lower than RN; RD was higher than RN in case of tryptic hydrolysis at pH 8.4 and 9.0. At initial stage of peptic and tryptic hydrolysis at neutral pH (RD > RN) the viscosity of hydrolyzate increased rapidly, suggesting the aggregation of enzymatically attacked albumin mols.This publication has 3 references indexed in Scilit:
- A NEW METHOD FOR THE COLORIMETRIC DETERMINATION OF ARGININEThe Journal of Biochemistry, 1950
- The Binding of Organic Ions by Proteins1Journal of the American Chemical Society, 1946
- Observations on the crystallizable albumin fraction of horse serumBiochemical Journal, 1938