Glycoprotein purification

Purification of a myeloma immunoglobulin M and its tryptic Fab and (Fc)j fragments Fractionation of soluble brain glycoproteins Purification of rat kidney glycoproteins for production of heterologous antisera which induce congenital abnormalities... 

Affinity chromatography of acid ribonuclease 268 from He La cell lysosomes demonstration that the enzyme is a glycoprotein Purification of human liver acid a-D- 148... 

Purification of pepsin glycopeptides from human immunoglobulin IgA myeloma glycoprotein Purification of porcine haptoglobin Purification of the serum prohormone of angiotensin Purification of the aa-trehalase from Saccharomyces cerevisiae Separation of different populations of membrane vesicles from thymocytes... 

N. Koide and T.Muramatsu, Endo-P-V-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae. J. 

Fibrinolytic effecting protease enzyme with glycoprotein structure relative mol mass ca. 30000. Isolation from the poison secretion (venom) of Agkistrodon rhodostoma (malayan pit viper) with chromatographic purification. 

While none of these neutrophil receptors has yet been sequenced, partial purification of the formyl peptide receptors has been reported (16). The formyl peptide receptor is particularly attractive because of the extensive structure-activity studies on peptide ligands by Freer and coworkers (17,18). The receptor is a trans-membrane glycoprotein with apparent molecular weight of 60,000 based on proteolysis (19) and photoaffinity (20) labeling studies. 

J Riordan, V Ling. (1979). Purification of P-glycoprotein from plasma membrane vesicles of Chinese hamster ovary cell mutants with reduced colchicine permeability. J Biol Chem 254 12701-12705. 

Sendai, Y., Abe, H., Kikuchi, M., Satoh, T. and Hoshi, H. (1995) Purification and molecular cloning of bovine oviduct specific glycoprotein. Biology of Reproduction 50, 927-934. 

Donohue-Rolfe, Arthur, David W.K. Acheson, Anne V. Kane, and Gerald T. Keusch. "Purification of Shiga Toxin and Shiga-Like Toxins I and II by Receptor Analog Affinity Chromatography with Immobilized PI Glycoprotein and Production of Cross-Reactive Monoclonal Antibodies." Infection and Immunity 57 (December 1989) 3888-893. 

Table 6.4 Some lectins commonly used in immobilized format for the purification of glycoproteins. The sugar specificity is listed, as are the free sugars used to elute the bound glycoprotein...

Crude protein sources containing one glycoprotein usually contain multiple glycoproteins. In most such instances, lectin-based affinity systems will result in the co-purification of several such glycoproteins. 

By means of gel electrophoresis on cross-linked, hydrolyzed starch,99 with simultaneous checking for proteins, lipids, and pectinesterase activity, it was found, however, that the product isolated after the separation on CM-Sephadex C-50 constitutes but one of five multiple forms of tomato pectinesterase, and is the one present in preponderant proportion98 (see Fig. 4). The accompanying lipid and sugar components were separated from this pectinesterase form in the course of the purification procedure. After analysis of the hydro-lyzate of the final product for fatty acids, as well as for carbohydrate components, it was possible to exclude the possibility of a lipoprotein,30 as well as glycoprotein,100 character of this form of tomato pectinesterase. 

Danbolt, N. C., Pines, G., and Kanner, B. I. (1990) Purification and reconstitution of the sodium- and potassium-coupled glutamate transport glycoprotein from rat brain. Biochemistry 29,6734-6740. 

Table III compares the biochemical features of the B-amylase which was purified to homogeneity from C. thermosulfurogenes (74). The enzyme is a tetrameric glycoprotein with an apparent molecular weight of 210,000. The thermophilic B-amylase binds tightly to raw starch presumably by glycoconjugate forces and it is still active while bound to starch (75). This feature has been used for improved affinity purification of the enzyme using raw starch (76).

Specialized Purification Procedures Purification of membrane proteins, 182, 499 purification of integral membrane proteins, 104, 329 reconstitution of membrane proteins, 104, 340 purification of DNA-binding proteins by site-specific DNA affinity chromatography, 182, 521 purification of glycoproteins, 182, 529 purification of multienzyme complexes, 182, 539. 

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