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Purification and partial characterization of an acid phosphatase from the body wall of sea cucumber Stichopus japonicus

Paper ID Volume ID Publish Year Pages File Format Full-Text
35487 45092 2009 5 PDF Available
Title
Purification and partial characterization of an acid phosphatase from the body wall of sea cucumber Stichopus japonicus
Abstract

A high molecular weight (HMW) acid phosphatase from the body wall of sea cucumber Stichopus japonicus was purified to homogeneity by a combination of anion exchange chromatography, gel filtration chromatography and high performance liquid chromatography (HPLC). The enzyme was purified 19.3-fold with a total yield of 1.2%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme showed a single protein band of MW 147.9 kDa. The enzyme displayed maximum activity at pH 4.0 and 50 °C with p-nitrophenyl phosphate as substrate. The enzyme activity appeared to be stable over pH 2.0–5.0 and up to 40 °C. The enzyme activity was enhanced slightly by Mg2+, whereas inhibited strongly by Cu2+ and Zn2+. The enzyme hydrolyzes several phosphate esters, suggesting a probable non-specific nature. The amino acid sequences of three segments of the purified enzyme were analyzed by mass spectroscopy, which did not have any homology with previously described acid phosphatase.

Keywords
Purification; Characterization; Sea cucumber (Stichopus japonicus); Acid phosphatase; Amino acid sequences; Autolysis
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Purification and partial characterization of an acid phosphatase from the body wall of sea cucumber Stichopus japonicus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 8, August 2009, Pages 875–879
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us