Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8360312 | Protein Expression and Purification | 2015 | 13 Pages |
Abstract
Osteoclastic protein tyrosine phosphatase (PTP-oc) is a structurally unique transmembrane protein tyrosine phosphatase (PTP) that contains only a relatively small intracellular PTP catalytic domain, does not have an extracellular domain, and lacks a signal peptide proximal to the NH2 terminus. The present study reports the expression, purification, and characterization of the intracellular catalytic domain of PTP-oc (ÎPTP-oc). ÎPTP-oc was expressed in Escherichia coli cells as a fusion with a six-histidine tag and was purified via nickel affinity chromatography. When with para-nitrophenylphosphate (p-NPP) as a substrate, ÎPTP-oc exhibited classical Michaelis-Menten kinetics. Its responses to temperature and ionic strength were similar to those of other PTPs. The optimal pH value of ÎPTP-oc is approximately 7.0, unlike other PTPs, whose optimal pH values are approximately 5.0.
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Biochemistry
Authors
Huan Jiang, Yuan Sui, Yue Cui, Peng Lin, Wannan Li, Shu Xing, Deli Wang, Min Hu, Xueqi Fu,