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• W2037398538 abstract "Biochemical and biological properties of Fcγ receptors isolated by the previously described five-step procedure from several different CLL patients cell lysates were investigated to gain insight into their structure-function relationship. The FcγR proteins isolated in a relatively homogeneous and biologically active form are a single polypeptide chain of mol. wt near 30,000 that starts with an amino terminal residue of glycine. Extensive reduction and alkylation did not change their mobility in SDS-PAGE, behavior during gel filtration, isoelectric points in 6 M urea, and amino acid compositions. Their amino acid compositions are essentially identical to each other, and are characterized by two readily alkylatable cysteinyl residues. FcγR proteins apparently lack glucosamine and galactosamine, which are the usual components of glycoproteins. The tryptic peptide maps of FcγR materials isolated from three different CLL patients cell lysates were found to be nearly identical to each other. The number of typtic peptides identified by ninhydrin staining were in good agreement with those expected from the total number of lysyl and arginyl residues estimated by amino acid analysis using the assumed mol. wt of 30,000 for FcγR materials. FcγR materials appeared to be associated with a mole of phospholipids as well as a mole of free fatty acid per mole of protein. The phospholipids associated with FcγR proteins were phosphatidyl-choline, -serine and -ethanolamine, which are the usual components of the plasma membrane of mammalian cells. Their association with FcγR proteins seems to be tight, since 70% of phosphorus associated with FcγR protein remained bound after delipidation and only phospholipase C treatment released about 75% of phosphorous from FcγR. The fatty acids extracted from two different FcγR materials were found by gas chromatography to be similar to each other and were composed of the usual membrane fatty acids (C16:0, C18:0 and C18:l). One preparation showed the association of a small but significant amount of arachiodonic acid (C20:4). Delipidation by chloroform-methanol as well as phospholipase C treatment did not affect the IgG-bincling capacity of FcyR materials." @default.
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• W2037398538 date "1981-01-01" @default.
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• W2037398538 title "Biochemical properties of biologically active Fcγ receptors of human B lymphocytes" @default.
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• W2037398538 doi "https://doi.org/10.1016/0161-5890(81)90048-1" @default.
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