Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease
Hayley A. Hanby,
X. Long Zheng
Issue:
Volume 1, Issue 3, August 2013
Pages:
43-50
Received:
8 August 2013
Published:
20 August 2013
Abstract: Here, we provide a comprehensive review of current findings concerning the biochemistry and physiological functions of ADAMTS7, a metalloprotease that is known to interact with cartilage oligomeric matrix protein, progranulin, and alpha2-macroglobulin. Such broad substrate specificity and potentially diverse physiological functions make ADAMTS7 an interesting enzyme to study. ADAMTS7 has been shown to play a role in the pathogenesis of arthritis and disc disorders. More recently, the ADAMTS7 locus is identified to have a strong association with coronary atherosclerotic disease. However, the role of ADAMTS7 in the development of atherosclerosis is yet to be determined. The development of an easy and high throughput assay for ADAMTS7 activity and appropriate animal models will allow us to uncover the novel mechanisms of coronary arterial disease.
Abstract: Here, we provide a comprehensive review of current findings concerning the biochemistry and physiological functions of ADAMTS7, a metalloprotease that is known to interact with cartilage oligomeric matrix protein, progranulin, and alpha2-macroglobulin. Such broad substrate specificity and potentially diverse physiological functions make ADAMTS7 an ...
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Immobilization of Cauliflower Myrosinase on Agar Agar Matrix and its Application with Various Effectors
Ajeet Kumar Rai,
Om Prakash,
Jagdish Singh,
Prabhakar Mohan Singh
Issue:
Volume 1, Issue 3, August 2013
Pages:
51-56
Received:
24 June 2013
Published:
30 August 2013
Abstract: The purified and thermo stable myrosinase from cauliflower seedlings was immobilized by 3.5% agar agar matrix and immobilized myrosinase chips were stored in extraction buffer. After 48 hours 30% enzyme activity was exuded into extraction media from immobilized enzyme chips. Effect of some metal ions and organic solvents on the activity of immobilized cauliflower myrosinase was studied. Amongst selective metal ions (Sr2+, Sn2+ and Ba2+), Sr2+ at 4 mM concentration exhibited marked activating effect on the activity up to 3 fold. However, Sn2+ and Ba2+ increased the activity to a certain extent and then suppressed. Activation kinetics of myrosinase in presence of Sn2+ and Sr2+ were studied between 0-20min.The rate of reaction was almost constant till 15 min and then slight deactivation was recorded at various concentrations used. On the other hand, few heavy metal ions [Fe2+, Fe3+, Cu2+ and Zn2+] strongly inhibited the activity even at lower concentrations. Several nonpolar organic solvents even at comparatively higher concentrations had detectable activation effects. Further, their activity was seen with respect totime (27 min). However, some protic polar organic solvents exhibited inhibitory effect with immobilized myrosinase except to butanol.
Abstract: The purified and thermo stable myrosinase from cauliflower seedlings was immobilized by 3.5% agar agar matrix and immobilized myrosinase chips were stored in extraction buffer. After 48 hours 30% enzyme activity was exuded into extraction media from immobilized enzyme chips. Effect of some metal ions and organic solvents on the activity of immobili...
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