Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
About: This article is published in Biochemistry.The article was published on 1971-06-22. It has received 8245 citations till now. The article focuses on the topics: Spectrin binding.
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TL;DR: Observations on the molecular basis of pleiotropic drug resistance are interpreted in terms of a model wherein certain surface glycoproteins control drug permeation by modulating the properties of hydrophobic membrane regions.
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TL;DR: This review focuses on work that deals with the mechanisms of detergent action in membrane solubilization including properties of detergents model lipid systems and detergent-protein interactions; in addition a possible sequence of events when deterGents interact with biological membranes receives attention.
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TL;DR: The findings suggest the possibility that Malignantly transformed fibroblasts lack surface fibronectin, which results in a lack of anchorage to the surrounding intercellular matrix, which could contribute to the malignant growth behavior.
Abstract: Fibronectin, a plasma protein immunologically identical with a major surface protein of normal fibroblasts, was found to bind to collagen and gelatin. A solid phase enzyme immunoassay was used for the binding tests. Collagen, gelatin or various control proteins were adsorbed to a plastic surface. Binding of fibronectin was detected using purified fibronectin antibodies conjugated to alkaline phosphatase. Circulating fibronectin and fibronectin obtained from fibroblast cultures both showed specific binding to collagen and gelatin. Preparative affinity chromatography of plasma on gelatin coupled to Sepharose gave electrophoretically and immunologically pure fibronectin in high yields. Malignantly transformed fibroblasts lack surface fibronectin. Our findings suggest the possibility that this results in a lack of anchorage to the surrounding intercellular matrix, which could contribute to the malignant growth behavior.
1,951 citations
TL;DR: This chapter considers only those lectins that have been purified to homogeneity, and studied with regard to their biophysical, biochemical, and carbohydrate-binding specificity.
Abstract: Publisher Summary Lectins play an important role in the development of immunology. Lectins also find application in serological laboratories for typing blood and determining secretor status, separating leucocytes from erythrocytes, and agglutinating cells from blood in the preparation of plasma. They serve as reagents for the detection, isolation, and characterization of carbohydrate-containing macromolecules, including blood-group antigens. In their interaction with saccharides, lectins serve as models for carbohydrate-specific antibodies, with the important advantage to purify lectins in gram quantities. Lectins are classified according to their carbohydrate-binding specificity that includes D-mannose(D-glucose)-binding lectins and 2-acetamido-2-deoxy-D-glucose-binding lectins. The chapter considers only those lectins that have been purified to homogeneity, and studied with regard to their biophysical, biochemical, and carbohydrate-binding specificity. The chapter also describes the cell-binding and biological properties of lectins. The chapter concludes with the description of several glycopeptide structures showing the carbohydrate-binding loci with which various lectins interact.
1,540 citations
TL;DR: This article will focus on the localization and modes of association of individual major polypeptides within the human red cell membrane.
Abstract: The elucidation of the molecular architecture of cell membranes is a central goal for cell biology, as structure lies at the heart of function. The erythrocyte plasma membrane has long provided a favored testing ground for this inquiry. Human red blood cells are readily available, relatively homogeneous, and relevant to medicine. Their plasma membranes can be easily isolated intact and essentially free of contamination from other cells, organelles, and cytoplasmic contents. This membrane is complex enough to be interesting and, to some degree, representative, yet it is simple enough to be analyzed as a whole. These circumstances make it likely that the human red cell plasma membrane will be the first whose molecular anatomy is known in any degree of satisfying detail. The literature concerning the proteins of erythrocyte membranes and membranes in general has been the subject of repeated review (1 9). This article will focus on the localization and modes of association of individual major polypeptides within the human red cell membrane.
1,452 citations
Cites background from "Electrophoretic analysis of the maj..."
...6% of the membrane mass is sialic acid (11, 18, 19, 76, 86)....
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...~ Calculated assuming this glycoprotein carries 70% of the membrane sialic acid (11, 50, 54) and that 1....
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...There is good evidence that (with one exception, see below) the components listed in Table I are not aggregates or complexes, since they cannot be reduced in size by a variety of dissociating agents; however, they are quite vulnerable to proteolytic degradation (11, 38)....
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...The PAS profile bears a close resemblance to the distribution of sialic acid in the gel, as determined by direct chemical analysis (11, 51, 52) and, more particularly, by the radioactivity profile of membrane proteins gently reacted with periodic acid (so as to oxidize only sialate residues) and then reduced by tritiated borohydride (53, 54)....
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...glycoproteins, are not readily detected by Coomassie blue and other conventional protein stains (4, 11), but are made visible by the periodic acidSchiff (PAS) staining technique (Fig....
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References
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TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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TL;DR: The technique of disc electrophoresis has been presented, including a discussion of the technical variables with special reference to the separation of protein fractions of normal human serum.
Abstract: Summary
The technique of disc electrophoresis has been presented, including a discussion of the technical variables with special reference to the separation of protein fractions of normal human serum.
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