Carbohydrate structure of glycopeptides isolated from an hepatic membrane-binding protein specific for asialoglycoproteins.

نویسندگان

  • T Kawasaki
  • G Ashwell
چکیده

Two variant glycopeptide constituents of an hepatic membrane protein responsible for the clearance of circulating asialoglycoproteins have been isolated and characterized. Their relative abundance has been estimated to be 14 and 2 mol, respectively, per mol of intact protein. The larger component, glycopeptide I, is comprised of sialic acid, galactose, mannose, glucosamine, and aspartic acid in a molar ratio of 3:3:2:5:1. The smaller neutral fraction contains only two sugars and the molar relationship of mannose, glucosamine, and aspartic acid is 8:2:1. Based on the results of sequential digestion with specific glycosidases and periodate degradation, a carbohydrate sequence for both glycopeptides is proposed.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Human Hepatic Lectin

We have isolated a human hepatic lectin with specificity for terminal Gal and GaINAc residues by affinity chromatography on p-aminophenyl-&D-tbiogalactosyl Sepharose. The human protein consists of a single subunit (Mr 41,000) as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The amino acid composition closely resembles that of the A and B subunits of the rabbit hepatic...

متن کامل

Occurrence of unique polysialosyl carbohydrate units in glycoproteins of developing brain.

A novel type of glycopeptides comprising approximately 10% of the total protein-bound neuraminic acid in developing rat brain have been isolated and characterized. The glycopeptides displayed unique properties including precipitation with cetylpyridinium chloride, strong binding to anion exchange column, and large apparent size in gel filtration. Structural studies including methylation analysi...

متن کامل

The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins.

The ability of hepatic plasma membranes to bind desialylated glycoproteins as a prelude to transport and catabolism has been reported earlier. The present study describes the purification, by affinity chromatography, of an hepatic protein which retains the characteristic binding properties associated with the membranes. The isolated material, which is watersoluble and free from lipids, has been...

متن کامل

Bi-and tri-antennary human transferrin glycopeptides and their affinities for the hepatic lectin specific for asialo-glycoproteins.

Glycopeptides were isolated from a proteolytic digest of human transferrin. After mild acid hydrolysis the desialylated glycopeptides were labelled by the galactose oxidase/NaB(3)H(4) procedure and then fractionated by Sephadex-gel filtration or by anion-exchange chromatography. Either technique allowed separation of the two heterosaccharide chains (designated glycan I and glycan II) previously...

متن کامل

Chemical and physical properties of an hepatic membrane protein that specifically binds asialoglycoproteins.

The state of aggregation found in water-soluble preparations of an hepatic membrane protein responsible for the clearance of serum asialoglycoproteins has been shown to result from the self-associating properties of a single oligomeric protein. The smallest functional unit identifiable in aqueous solution possessed an estimated molecular weight of 500,000 with each of the successive components ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 251 17  شماره 

صفحات  -

تاریخ انتشار 1976