The 102 kDa chicken liver acid phosphatase: Dimeric structure, glycoprotein nature and immunological properties agata szalewicz, teresa grabska, and aleksandra kubicz

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 117, Issue 2, 1997, Pages 293-298

  Szalewicz, Agata ^a   Grabska, Teresa ^a   Kubicz, Aleksandra ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Acid phosphatase; Enzyme Heterogeneity; Glycoen zymes; Glycoproteins; High molecular weight acid phosphatase

Indexed keywords

ACID PHOSPHATASE; CARBOHYDRATE; GLYCOPROTEIN; LECTIN; SUGAR;

ANIMAL TISSUE; ARTICLE; CHICKEN; IMMUNOBLOTTING; ISOELECTRIC FOCUSING; LIVER; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ANIMALIA; ANURA; CYPRINUS CARPIO; GALLUS GALLUS;

EID: 0030749475     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(97)00090-4     Document Type: Article

References (14)

1. Jańska, H.; Kubicz, A. Studies on the heterogeneity of carp liver acid phosphatases: Acid Phosphatase I - subunit structure and carbohydrate composition. Comp. Biochem. Physiol. 82B:563-567;1985.
2. Jańska, H.; Kubicz, A.; Bem, M.; Van Etten, R.L. Catfish liver acid phosphatase: Differently glycosylated enzyme molecules with altered kinetic properties. Comp. Biochem. Physiol. 85B: 753-758;1986.
3. Jańska, H.; Kubicz, A.; Szalewicz, A.; Haraźna, J. The high molecular weight and the low molecular weight acid phosphatases of the frog liver and their phosphotyrosine activity. Comp. Biochem. Physiol. 90B:173-178;1988.
4. Kubicz, A.; Szalewicz, A.; Chrambach, A. Studies on the oligosaccharide heterogeneity of the isoelectric forms of the lower molecular weight acid phosphatase of frog liver. Int. J. Biochem. 23:413-419;1991.
5. Kubicz, A.; Szalewicz, A. Characterization of the type of carbohydrate chains of the higher molecular weight (140 kDa) acid phosphatase of the frog liver. Int. J. Biochem. 25:1957-1961;1993.
6. Laemmli U.K. Cleavage of structural protein during the assembly of the head of the bacteriophage T4. Nature 227:680-685;1970.
7. Lowry, O.H.; Rosebrough, N.J.; Farr, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 143:265-275;1951.
8. Merril, C.R.; Goldman, D.; Sedman, S.A.; Ebert M.H. Ultrasensitive stain for proteins in polyacrylamide gels shows variation in cerebrospinal fluid proteins. Science 211:1437-1438; 1981.
9. Osawa, T.; Tsuji, T. Fractionation and structural assessment of oligosaccharides and glycopeptides by use of immobilized lectins. Ann. Rev. Biochem. 56:21-42;1987.
10. Panara F. Isolation and partial characterization of high and low molecular weight acid phosphatases from chicken liver. Int. J. Biochem. 17:1213-1217;1985.
11. Panara, F.; Mileti, A. Subcellular localization of high- and low-molecular weight acid phosphatases from chicken liver. Int. J. Biochem. 18:1057-1059;1986.
12. 2+-dependent acid p-nitrophenyl phosphatase from chicken liver. Purification, characterization and subcellular localization. Int. J. Biochem. 20:457-462;1988.
13. Szalewicz, A., Jańska, H., Strzelczyk, B.; Kubicz, A. Amino acid composition and immunochemical properties of AcPase III and AcPase IV representing glycoforms of the lower molecular, tartrate resistant acid phosphatase of the frog liver. Int. J. Biochem. 24:975-979;1992.
14. Towbin, H.; Staehelin, T.; Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354;1979.