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Abstract

SUBCELLULAR DISTRIBUTION AND PURIFICATION OF HEAT SHOCK PROTEIN 90 IN SHEEP LIVER TISSUE

Rifat Ara, Ruqaya Aziz, Shazia Nazir, Aeijaz Ul Noor, Khurshid I Andrabi

ABSTRACT

Heat shock proteins are a group of highly conserved proteins that are constitutively expressed in most cells under normal physiological conditions.HSP90 has been identified in the cytosol, nucleus and, endoplasmic reticulum, and is reported to exist in many cell types. To obtain large amount of HSP 90 and examine the properties of the purified protein, tissues may be better as materials for purification than cultured cells. The 90KDa heat shock protein (HSP90) has been purified from mammalian tissues(sheep liver) with a good yield by a method involving DEAE-cellulose chromatography, and its subcellular localization in different organelles reveals that HSP90 is a highly conserved protein during evolution. Our present study examines the constitutive expression of HSP90 in various subcellular fractions of liver tissue by immunobloting and its purification by conventional chromatographic techniques

Keywords: Hsp, DEAE, Sheep liver, chromatography.


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