WORKING HOURS

7 Days a Week from 24 Hours

Edit
Online Resources
Learn more about different online health resources offered by Giostar India, including appointment, and more.
EXPRESS CARE ONLINE

Get a diagnosis and prescription virtually, from the comfort of your own home or office.

My Chart

View portions of your medical record, see test results, renew prescriptions and more.

My Consult

View portions of your medical record, see test results, renew prescriptions and more.

Purification and properties of cytosolic alanine aminotransferase from the liver of two freshwater fish, Clarias batrachus and Labeo rohita.

Srivastava AS, Oohara I, Suzuki T, Shenouda S, Singh SN, Chauhan DP, Carrier E. Comp Biochem Physiol B Biochem Mol Biol. 2004 Feb;137(2):197-207.

Abstract

Cytosolic alanine aminotransferase (c-AAT) was purified up to 203- and 120-fold, from the liver of two freshwater teleosts Clarias batrachus (air-breathing, carnivorous) and Labeo rohita (water-breathing, herbivorous), respectively. The enzyme from both fish showed similar elution profiles on a DEAE-Sephacel ion exchange column. SDS-PAGE of purified enzymes revealed two subunits of 54 and 56 kDa, in both fish. The apparent Km values for l-alanine were 18.5+/-0.48 and 23.55+/-0.60 mM, whereas for 2-oxoglutarate the Km values were observed to be 0.29+/-0.023 and 0.33+/-0.028 mM for the enzyme from C. batrachus and L. rohita, respectively. With l-alanine as substrate, aminooxyacetic acid was found to act as a competitive inhibitor with KI values of 6.4 x 10(-4) and 3.4 x 10(-4) mM with c-AAT of C. batrachus and L. rohita, respectively. However, when 2-oxoglutarate was used as substrate, aminooxyacetic acid showed uncompetitive inhibition with similar KI values for purified c-AAT from both fish.

Appointment Details