Arylsulphatase C activity of sheep liver & brain under different conditions of solubilization
Lakshmi, S.; Balasubramanian, A.S.
Indian Journal of Biochemistry and Biophysics 18(1): 36-39
1981
ISSN/ISBN: 0301-1208 PMID: 6944270 Document Number: 181621
Arylsulfatase C of sheep liver microsomal fraction was solubilized by the chaotrope KSCN and its properties compared with the arylsulphatase C solubilized from the sheep brain acetone powder in a similar fashion. The activity of the solubilized liver enzyme was enhanced by the antichaotropes, (NH4)2SO4 and sodium citrate. Dialysis of the solubilized ammonium sulphate fraction of the enzyme resulted in a significant loss of activity, but, unlike the brain enzyme, the activity could be regained by the addition of antichaotropes and there was no evidence for the requirement of a dialyzable activator for restoration of activity. Similar results were obtained using the acetone powder of sheep liver microsomes for solubilization. Solubilization of the brain or liver enzyme with a nonionic detergent, Triton X 100 and NaCl, gave a preparation which did not lose any significant activity on dialysis or gel filtration. On Sephadex G-200 gel filtration, the Triton solubilized enzymes emerged as high MW components. Apparently hydrophobic interactions influence the arylsulphatase C of both brain and liver. But the micro-environment of the enzymes from the 2 organs might vary whereby the chatropically-solubilized brain enzyme exhibited the need for a dialyzable activator for optimal activity while the liver enzyme did not require any dialyzable activator.