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Biomedical subjects

A Spector

Publications and source records attributed to A Spector.

At least 127 records · Page 7Linked to original sources
PubMed1982

Lens plasma membrane: isolation and biochemical characterization.

Lens plasma membrane from different animal lenses has been prepared by the acylation procedure. Using three different criteria: heat aggregation of intrinsic membrane polypeptides, immunochemistry and solubilization of intrinsic proteins at low (40 mM) LIS concentration, it has been shown that these preparations are essentially free of cytoplasmic contaminants. Using the results obtained with acylated membrane as the reference of purity, it has been shown that both sucrose gradient centrifugation of bovine WI protein and urea washing of old human lenses give impure membrane preparations. The main intrinsic polypeptides (mol. wt 26 000 and 22 000) of human lens membrane have been purified and characterized. It has been shown by enzymatic digestion and amino terminal analysis of the residual membrane-bound fragments that the amino terminal halves of the polypeptides are embedded in the lipid bilayer and are probably blocked at their amino terminal sites. Lipid analyses of human and bovine lens membranes suggest that the protein to total lipid ratio is 1:1. Carbohydrate analyses of chromatographically separated intrinsic membrane polypeptides indicate the presence of 1 mol glucose/1 mol protein.

Amino Acids↗
PubMed1981

Biochemical evidence for membrane disintegration in human cataracts.

Biochemical evidence is presented for the disintegration of the lens fiber plasma membrane in human cataracts. The intrinsic membrane proteins are found in both the water-soluble and water-insoluble nonmembrane fractions of the cataract lens but not in the normal tissue. Furthermore, in contrast to the normal lens, not all of the lipid found in the cataractous lens is isolated with the membrane fraction. In cataracts, both the membrane and membrane fragments are involved in covalent high molecular weight aggregates with an extrinsic membrane protein (43,000 daltons) and a cytoplasmic protein (gamma-crystallin).

Amino Acid Sequence↗
PubMed1980

Selective oxidation of cysteine and methionine in normal and senile cataractous lenses.

The oxidation state of methionine and cysteine in normal and cataractous lenses is reported. In young lenses no oxidation was detected in any protein fraction examined. Only the intrinsic membrane fraction and membrane-related components showed evidence of oxidation in old (60-65 years of age) normal lenses. However, in a similar age group, with the development of cataract, progressive, dramatic changes were observed. With severe cataracts, 60% or more of the methionine in membrane-associated components was found in the methionine sulfoxide form, and methionine sulfone was observed in one case. Most of the cysteine was found oxidized to either the disulfide form or putative cysteic acid. Mixed disulfides with glutathione were observed. Oxidative changes in soluble components as illustrated by alpha-crystallin occurred more gradually. The data clearly support the viewpoint that extensive oxidation of lens proteins occurs with cataract and that it begins at the lens fiber membrane.

Aged↗
PubMed1979

An extrinsic membrane polypeptide associated with high-molecular-weight protein aggregates in human cataract.

A 43,000-dalton polypeptide has been isolated from the high-molecular-weight disulfide-rich fraction of the water-insoluble protein of human cataractous lenses. On the basis of immunochemical reactivity and fluorescent antibody binding, this polypeptide is localized in the membrane region of the lens cell. This observation suggests an interaction between the soluble lens proteins and membrane-associated polypeptides in the formation of large protein aggregates which may cause cataract.

Antibody Specificity↗