Disposition of the major proteins in the isolated erythrocyte membrane. Proteolytic dissection

Steck, Theodore L.; Fairbanks, Grant; Wallach, Donald F. Hoelzl

doi:10.1021/bi00789a031

Cited by 302 publications

(101 citation statements)

References 17 publications

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“…4a; Steck et al, 1971). When intact erythrocytes were digested by trypsin under the same conditions but at low ionic strength (in 300mM-sucrose containing 5mM-sodium phosphate buffer, pH 8.0), 55 % of the polypeptide 3 was cleaved to give a product ofmol.wt.…”

Section: Radioiodination Of the Extracellular Regions Ofpolypeptidesmentioning

confidence: 99%

Ionic-strength-dependent changes in the structure of the major protein of the human erythrocyte membrane

Jenkins¹,

Tanner²

1977

Biochemical Journal

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The effect of ionic strength on the proteolysis by trypsin of the major membranepenetrating protein (polypeptide 3) in the erythrocyte membrane was studied. Both the intracellular and extracellular regions of the protein are susceptible to trypsin proteolysis under hypo-osmotic conditions, whereas under iso-osmotic conditions the extracellular region of the protein is resistant to trypsin, and the intracellular region yields only two cleavage products with trypsin. Studies of the fragments obtained from polypeptide 3 by trypsin digestion under iso-osmotic conditions of 'ghosts' radioiodinated with lactoperoxidase confirmed our earlier conclusions that the polypeptide chain of polypeptide 3 traverses the membrane twice. Ionic-strength-dependent changes were also observed in the incorporation of iodine by lactoperoxidase into the individual extracellular tyrosine sites of the protein. These results show that polypeptide 3 undergoes ionic-strength-dependent changes in structure.

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Section: Radioiodination Of the Extracellular Regions Ofpolypeptidesmentioning

confidence: 99%

Ionic-strength-dependent changes in the structure of the major protein of the human erythrocyte membrane

Jenkins¹,

Tanner²

1977

Biochemical Journal

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show abstract

“…The molecular weight distribution of these membrane proteins is similar to that observed on 5% gels. Molecular weight classes of proteins from 200,000 to 20,000 are present as previously reported [ 1,4,7,8] .…”

Section: Resultsmentioning

confidence: 72%

“…1 has been stained for carbohydrate and four bands are clearly visible, corresponding to molecular weights of 62,000, 34,000, 29,000 and 14,000, respectively. The 14,000 molecular weight material, which has been reported by various investigators to be lipid [7] or glycolipid [8], stains abnormally and may not be a glycoprotein. Gel B in the figure has been stained for protein with Coomassie blue.…”

Section: Resultsmentioning

confidence: 82%

“…This component has recently been identified as a glycoprotein [ 161 and appears to be the same molecule which is iodinated as suggested by Steck [8]. The difference in the molecular weight determinations may be due to anomolous electrophoresis of the glycoprotein.…”

Section: Discussionmentioning

confidence: 89%

“…However, since the carbohydrates can be removed by proteolytic hydrolysis [8,9,13,141 and are also substrate for lactoperoxidase, a reasonable portion of the polypeptide chain must be exposed on the membrane surface in addition to the carbohydrate residues.…”

Section: Discussionmentioning

confidence: 99%

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