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CLC number: R779.6

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Received: 2007-03-14

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Journal of Zhejiang University SCIENCE B 2007 Vol.8 No.8 P.599-603

http://doi.org/10.1631/jzus.2007.B0599


Comparison in effect of different metal ions, pH and reducing agent on the protease activity in human hyper mature and mature cataract


Author(s):  SAMI Amtul Jamil, SAMI Amtul Naseer, KANWAL Noreen

Affiliation(s):  Institute of Biochemistry and Biotechnology, University of the Punjab, Lahore 54594, Pakistan; more

Corresponding email(s):   amtulljamil@yahoo.com

Key Words:  Mature cataract, Hyper mature cataract, Eye lens, Protease activity, &beta, mercaptoehanol


SAMI Amtul Jamil, SAMI Amtul Naseer, KANWAL Noreen. Comparison in effect of different metal ions, pH and reducing agent on the protease activity in human hyper mature and mature cataract[J]. Journal of Zhejiang University Science B, 2007, 8(8): 599-603.

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author="SAMI Amtul Jamil, SAMI Amtul Naseer, KANWAL Noreen",
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%J Journal of Zhejiang University SCIENCE B
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%I Zhejiang University Press & Springer
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A1 - SAMI Amtul Jamil
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A1 - KANWAL Noreen
J0 - Journal of Zhejiang University Science B
VL - 8
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PB - Zhejiang University Press & Springer
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DOI - 10.1631/jzus.2007.B0599


Abstract: 
This study was undertaken to isolate and characterize the protease activity of human eye lens sample of mature and hyper mature cataract. Samples were collected just after surgery of the cataract lens and were stored at −20 °C. The total protein extract was isolated from 5 samples in each case (mature and hyper mature cataract) and clear supernatant obtained after centrifugation was used as an enzyme source. The optimum pH for the proteases of mature cataract was 7.5 while the proteases of hyper mature cataract were recorded for maximum activity at pH 5.5 and 7.5. The optimum temperature for both enzyme sources was 50 °C. Effect of different metal ions such as potassium, lead, silver, zinc and borate was studied. In each case protease activity was increased. Reducing agent e.g. &beta; mercaptoethanol also caused an increase in activity indicating the involvement of sulfhydryl groups. protease activity was also located on agar plates.

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Reference

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[5] Sami, A.J., Kanwal, N., Sami, A.N., 2006. Detection of Two Distinct Proteases Activities in Hyper Mature Human Cataract Eye Lens. Abstract No. 559, Bioscience 2006. Biochemical Society Meeting, 23-27 July, Glasgow, UK.

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[8] Sulochana, K.M., Ramakrishnan, S., Arunagri, K., 1996. Purification and characterization of a new enzyme dipeptidase from human lens. Exp. Eye Res., 62(3):221-229.

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