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R V Prasad

Publications and source records attributed to R V Prasad.

5 recordsLinked to original sources

Conformational studies on rat alpha-lactalbumin.

The reversible unfolding of rat alpha-lactalbumin, which, in contrast to other alpha-lactalbumins, has a 17-amino-acid extension at the carboxyl terminus and a carbohydrate unit at Asn-45, was studied by circular dichroism between 193 and 310 nm as a function of pH, heat and guanidine hydrochloride ( GdnHCl ). The native structure of rat alpha-lactalbumin was similar to that of bovine alpha-lactalbumin. Acidification changes rat alpha-lactalbumin to a state similar to the 'A state' of bovine alpha- lactalbumin . The heat-reduced unfolding of the tertiary structure of rat alpha-lactalbumin is highly cooperative. The GdnHCl -induced unfolding of rat alpha-lactalbumin could not be expressed by a two-state mechanism as in the case of bovine alpha-lactalbumin. However, the midpoints of transitions suggested lower stabilities of secondary and tertiary structures in rat alpha-lactalbumin than in bovine alpha-lactalbumin consistent with the differences in the local structure between rat and bovine alpha-lactalbumins.

Animals↗

Amino acid sequence of rat alpha-lactalbumin: a unique alpha-lactalbumin.

The amino acid sequence of rat alpha-lactalbumin has been determined. Unlike other alpha-lactalbumins which contain 122 or 123 amino acids, rat alpha-lactalbumin is unique in that it contains 140 amino acids. The extra amino acids are a 17 amino acid extension at the carboxyl terminus. The amino acid sequence of this extension is Gly124-Ala-Pro-Ala-Leu-Val-Val130-Pro-Ala-Leu-Asp-Gly135-Glu-Thr-Pro-Val-Pro140 . The extension is proline rich, which may contribute to the anomalous structural properties of rat alpha-lactalbumin. The amino acid sequence from residues 1 to 123 is similar to that of other alpha-lactalbumins. One possible explanation for the 17 amino acid extension is a mutation at the termination codon.

Amino Acid Sequence↗

Isolation and characterization of alpha-lactalbumin from a rat mammary tumor.

alpha-Lactalbumin was purified to homogeneity from the R3230AC rat mammary adenocarcinoma. alpha-Lactalbumin from the R3230AC tumor had the same amino acid and carbohydrate composition, migration on gel electrophoresis, and specific activity as did alpha-lactalbumin isolated from normal rat milk.

Adenocarcinoma↗

Transfer factor therapy in hyperimmunoglobulinaemia E syndrome.

The therapeutic effect of transfer factor (TF) from healthy donors was investigated in two children with extensive intractable atopic dermatitis, recurrent pyogenic skin infections, hyperimmunoglobulinaemia E, defective neutrophil chemotaxis and depressed cell-mediated immunity. Striking clinical improvement was noted in both patients with disappearance of skin infections, pruritus and eczema. No new lesions have occurred 13 months after the completion of therapy in the first patient but a few new atopic lesions have reappeared after 8 months in the second. Both patients are off steroids and antibiotics. Transfer factor administration did not influence the T cell rosette number or the lymphocyte blastic transformation response, but it did cause conversion of the skin-test reactivity in both patients and correction of polymorphonuclear chemotaxis in one of them. Non clinical side-effects were noted but marked and persistent rise of serum IgE was observed in both patients. Our data suggest that patients with hyper-IgE syndrome may be benefited by TF therapy and they lend further support to the notion that T lymphocyte deficiency may be the basis of the eczema in this syndrome.

Antibody Formation↗