Partial purification and some properties of aspartate aminotransferase from the mantle tissue of Mytilus galloprovincialis Lam.

Yurtpinar O. D., Ozden T. Y., Can A.

ISTANBUL JOURNAL OF PHARMACY, cilt.44, sa.1, ss.1-10, 2014 (ESCI) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 44 Sayı: 1
  • Basım Tarihi: 2014
  • Dergi Adı: ISTANBUL JOURNAL OF PHARMACY
  • Derginin Tarandığı İndeksler: Emerging Sources Citation Index (ESCI)
  • Sayfa Sayıları: ss.1-10
  • Anahtar Kelimeler: aspartate aminotransferase, Mytilus galloprovincialis Lam., mussel, enzyme purification
  • İstanbul Üniversitesi Adresli: Evet

Özet

Aspartate aminotransferase (E.C.2.6.1.1; AST), is a pyridoxal phosphate dependent enzyme that occurs in virtually all organisms and plays a key role in intermediary nitrogen metabolism. Although AST was purified from a variety of plant and animal sources, it has not been purified previously from mantle tissue of Mytilus galloprovincialis Lam. In the present study we have partially purified AST from the mantle tissue of M. galloprovincialis and investigated some kinetic properties of the enzyme. The partially purified enzyme showed three protein and a single activity band in polyacrylamide gel electrophoresis. It was found that the enzyme exhibited maximum activity at 15 degrees C and 35 degrees C and that the activity was decreased at 40 degrees C and totally lost at 55 degrees C. AST activity was maximum at pH 7.4 in Tris-HCl buffer. Km values of AST for aspartate and 2-oxoglutarate were 1.64 mM and 2.2x10(-2) mM, respectively, and Vmax values for the same substrates were 0.12 U/mL and 0.168 U/mL, respectively.