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At least 1,423 records · Page 79Linked to original sources
PubMed1977

The denaturation of beta-lactoglobulin-A at pH 2.

The denaturation of beta-lactoglobulin-A by heat and guanidine hydrochloride at pH 2 has been investigated. The effect of ethylene glycol on the thermal denaturation at this pH has also been studied. The conditions of the experiments have been chosen so as to eliminate complications arising out of disulfide interchange, changes in the degree of association of the protein during denaturation, and intermolecular aggregation. The physical parameters characterizing the denatured states of the protein which are produced by heat and guanidine hydrochloride have been determined. The thermodynamic parameters for these transitions have been estimated using a two-state hypothesis in each case. Both the physical and thermodynamic parameters indicate that the heat-denatured state of beta-lactoglobulin-A retains about 15-20% of residual structure which is destroyed on adding guanidine hydrochloride.

Circular Dichroism↗
PubMed1978

Conformation of a stable intermediate on the folding pathway of Staphylococcus aureus penicillinase.

The partly unfolded intermediate (state H) of penicillinase from Staphylococcus aureus PC1 is stable in 0.8 M guanidinium chloride at pH 7.0. It has been characterized by measurements of intrinsic viscosity, sedimentation and diffusion coefficients, leading to an equivalent hydrodynamic volume of five times that of the native penicillinase molecule. Values of alpha-helix content calculated from circular dichroism were 27% for penicillinase and 16% for state H. A multi-domain model is proposed for penicillinase in which the domains can separate without appreciable change in secondary structure. This model is important in understanding the means by which the enzyme activity can be controlled, and corresponds to a kinetic pathway of folding.

Circular Dichroism↗
PubMed1981

The hexa- and pentapeptide extension of proalbumin. I. Chemical synthesis of serum albumin propeptides.

The proalbumin hexapeptide extension was synthesized beginning from the C-terminal end by stepwise N-terminal peptide chain elongation starting from N-tert-butyloxycarbonyl-(Ng-nitro)arginyl-(Ng-nitro)arginine 4-nitrobenzyl ester; [alpha](20)365-12 degrees C (c = 1; dimethylformamide). The other amino acids were incorporated by excess mixed anhydrides of Ddz-amino acids (Ddz; 3,5-dimethoxyphenylisopropyloxycarbonyl) yielding the fully protected hexapeptide in crystalline quality. After removal of the protective groups by acid treatment and hydrogenation the peptide was purified by Dowex ion-exchange and Sephadex chromatography. The purity was confirmed by thin-layer chromatography and amino acid analysis.

Animals↗
PubMed1981

Purification and characterization of four components of rat caseins.

Rat casein components (C1-, C3A-, C3B- and C4-casein) were extensively purified from rat milk, and the properties of these proteins were compared with those of other caseins including rat C2-casein. C1-casein was precipitated by a low concentration of CaCl2 (1.5 mM). Both C3A- and C3B-casein were less sensitive to Ca2+ than were C1- and C2-casein, and the presence of 20 mM CaCl2 was required at 37 degrees C for their precipitation. C4-casein was absolutely insensitive to Ca2+. This protein exhibited the ability to stabilize all of the other rat casein components against Ca2+-dependent precipitation. In addition, C4-casein contained sialic acid, galactose and N-acetylgalactosamine. Therefore, C4-casein appears to be a bovine kappa-casein-like protein.

Amino Acids↗