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- W2009701344 abstract "Complete amino acid analyses of purified Clq from human serum indicate that this glycoprotein has an unusual composition for a serum protein, which includes hydroxyproline, hydroxylysine and high levels of glycine. A majority of the hydroxylysine residues are resistant to periodate oxidation; presumably they are protected by linkages to carbohydrate groups. In addition the total carbohydrate content is 7.7%, consisting primarily of glucose and galactose in equimolar amounts. Smaller quantities of sialic acid, fucose, mannose, galactosamine and glucosamine were also found. Thus, the data indicate that Clq has a structural similarity to collagen and collagen-like proteins." @default.
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- W2009701344 date "1971-06-01" @default.
- W2009701344 modified "2023-10-12" @default.
- W2009701344 title "Chemical studies on Clq; A modulator of immunoglobulin biology" @default.
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- W2009701344 doi "https://doi.org/10.1016/s0006-291x(71)80028-1" @default.
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