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1992 | 39 | 2 |

Tytuł artykułu

Molecular basis for the functional diversity of enzyme forms of the LMW [Mr 38000] acid phosphatase of the frog liver

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Recent studies on the structure and function of the tartrate-resistant acid phosphatase (Mr 38 000) of the frog liver arc reviewed. The nature of the enzyme heterogeneity is elucidated on a molecular and physiologi­cal basis. The following structure-activity relationship is proposed: the enzyme protein is modified by glycosylation processes leading to forma­tion of the different enzyme forms. The oligosaccharide chain stabilizes the final structure of the enzyme forms with altered conformation causing different exposure of the essential functional groups (e.g. sulfliydryl residues, antigen determinants). This leads to different physiological events necessary for fulfillment of metabolic requirements of the cell.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

39

Numer

2

Opis fizyczny

p.165-176,fig.

Twórcy

autor
  • University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland

Bibliografia

  • 1. Di Pctro, D. L. & Zcngcrle, F. S. (1967) Separation and properties of three acid phosphatases from human placenta../. Biol. Chem., 242, 3391 - 3396.
  • 2. Filburn, C. R. (1973) Acid phosphatase isoenzymes of Xenopus laevis tadpole tails. I. Separation and partial characterization. Arch. Biochem. Biophys., 159,683 - 693.
  • 3. Uiwrcnce, G. L. & Van Etten. R. (1981) Hie low molecular weight acid phosphatase from bovine liver, isolation, amino acid composition, and chemical modification studies. Arch Biochem. Biophys., 206, 122- 131.
  • 4. Baxter, J. II. & Suelter. C. H. (1985) Resolution of the low-molecular weight acid phosphatase in avian pectoral muscle into distinct enzyme forms. Arcli. Biochem. Biophys., 240, 134- 145.
  • 5. Panara. F. (1985) Isolation and partial characterization of high and low molecular weight acid phosphatases from chicken liver. Int. J. Biochem.. 17,1213 - 1217.
  • 6. Murakami, K. M„ Fujimoto. S. & Ohara. A. (1986) Subcellular localization and some properties of intermcdiate-molecular-wcight acid phosphatase from liver. Cham. ¡'harm. Bull., 34,3320 - 3327.
  • 7. Kubicz, A., Wahccd, A. & Van Etten, R L. (1985) Isolation and characterization of a homogeneous acid phosphatase from catfish liver. Comp. Biochem. Physiol., 81 B, 177 - 183.
  • 8. Jartska, H.t Kubicz, A., Bern, M. & Van Etten, R. L. (1986) Catfish liver acid phosphatase: differently glycosylated enzyme molecules with altered kinetic properties. Comp. Bioch. Physiol.. 85 B, 753 - 758.
  • 9. Kubicz, A., Dratcwka-Kos, E. & Zygmuntowicz, R. (1981) Multiple molecular forms of the acid phosphatase from Cyprinus carpio liver: isolation and comparison with those of Rana esculenm. Comp. Bioch. Physiol., 6K B, 437 - 443.
  • 10. Jartska, H. & Kubicz, A. (1985) Studies on U»c heterogeneity of the carp liver acid phosphatases; acid phosphatase I - subunit structure ;md carbohydrate composition. Comp. Biochem. Physiol82 B, 563 - 567.
  • 11. Jartska, H., Kubicz, A.. Szalewicz, A. & Harazna, J. (1988) Hie high molecular weight and low molecular weight acid phosphatases of the frog liver and their phosphotyrosine activity. Comp. Bioch. Physiol., 90 B, 173 -178.
  • 12. Mar/, I.. Hailon, M. W. C. (1984) A proposal: that die heterogeneity of glycoprotein N-glycans is a feature of their biosynthesis and may be of functional significance. Int. J Biochem.. 16, 253 - 256.
  • 13. Sairam, M. R. (1989) Role of carbohydrate in glycoprotein honnone signal transduc­tion FASEBJ.. 3, 1915- 1926.
  • 14. Kubie/., A., Dratewka, R & Malicka-Hłaszkiewicz. M. (1978) Acid phosphatase from liver of the frog Rana esculenta, separation and partial characterization of multiple forms. Acta liiochim Polon.. 25,349 - 359.
  • 15. Szalewicz, A.. Jariska. H., Strzelczyk. B. & Knhicz, A. (1992) Amino acid composi­tion and immunochemical properties of AcPasc III and AcPasc IV representing glycoforms of the lower molecular weight, tartratc-rcsistani acid phosphatase of the frog liver. Int. J. I Hoc hem.. 24.975 - 979.
  • 16. Jariska, H.. Kubicz, A. & Szalewicz, A. (1989) lite lower molecular weight acid phosphatase from die frog liver: isolation of homogeneous AcPasc III and IV representing glycofonus with different hioadivity. Comp. Hiochem Physiol.. *>2 B, 341 - 316.
  • 17. Knhicz, A , Szalewicz, A , I 'awcett. J. S. & Chrambach. A. (1990) Hlccuofocusing of acid phosphatase from frog liver using iin immobilized pi I gradient. Electrophoresis, 11, 117-151-
  • 18. Kubicz. A., Szalewicz, A. & Chrambach, A. (1991) Studies on the oligosaccluuide heterogeneity of tlie isoelectric fonns of Uie lower molecular weight acid phosphatase of frog liver. Int. J. Biochem., 23,413-419.
  • 19. Manjunath. P. & Sairam, M. R. (19X3) linhanced thermal stability of chemically deglycosylatcd hunuui choriogonadotropin../. Biol. Chern., 258, 3554 - 3558.
  • 20. Ostrowski, W. S. (19SS) Kwaśna fosfataza ludzkiego gruczołu krokowego Os­solineum - PAN, Wrocław-Warszawa- Kraków-Gdańsk-Łódź.
  • 21. Twardowski, J„ Nowak. I., Slufkcns, I). J. & Snocck, 'I'. L. (19X4) Laser Raman spectroscopy of acid phosphatases from rat liver. Biopolxmers, 17, 181 - 190.

Typ dokumentu

Bibliografia

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Identyfikator YADDA

bwmeta1.element.agro-article-9dc5e53d-db57-4219-a939-81372cbf4135
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