A crystalline glycopeptide from normal human urine

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A crystalline glycopeptide from normal human urine.

There is abundant evidence that glycosaminoglyeans are linked covalently to the protein in tissues (Mathews & Lozaityte, 1958; Muir, 1958). This fact suggested that isolation and characterization of glycosaminoglycan-peptides, particularly uronic acid-containing glycopeptides in normal urine, will assist in the understanding of the normal metabolism of glycosaminoglycans in tissues. The present...

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The isolation of crystalline erythritol from normal human urine.

With the finding that xylitol is an intermediate in the glucuronate-xylulose pathway (2, 3)) experiments were undertaken to determine whether this pentitol occurs in human urine. Instead of xylitol, the analyses led to the isolation of n-arabitol from pentosuric urine as well as nL-arabitol from normal urine (4). During the fractionation of urinary polyols on Dowex l-borate columns, eluates wer...

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A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.

A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine. The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis. The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine. Sugar analysis and amino acid analysis gave eq...

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Characterization of Antibodies in Normal Human Urine.

Certain of the physiochemical and immunochemical properties of the y-globulins of normal human urine have been reported by Webb, Rose, and Sehon (2) and by Franklin (3). These urinary proteins were found to be electrophoretically and antigenically closely related to serum y-globulins, but smaller in size; their molecular weights ranged from 10,600 (2) to 38,000 (3). Sedimentation coefficients S...

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The Structure of a Glycopeptide from Human Orosomucoid

Four glycopeptides were isolated from desialized orosomucoid following digestion with Pronase and chromatography on sulfoethyl cellulose. The structure of the major glycopeptide was studied with sequential hydrolysis with /3galactosidase, /3-acetylglucosaminidase, and a-mannosidase, as well as by oxidation with periodate. Evidence for a glycosylamine type linkage between aspartic acid and acety...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1969

ISSN: 0306-3283

DOI: 10.1042/bj1120379