Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii.

Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Research Abstract Details 

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Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Abstract Text:

Y Kuwabara,M Maruyama,Y Watanabe,S Tanaka,M Takakuwa,Y Tamai,

Membrane-bound phospholipase B was purified to a homogeneous state from Torulaspora delbrueckii cell homogenate. Cell homogenate was extracted with Triton X-100, and the enzyme was precipitated with acetone. The acetone powder was washed repeatedly with Tris-HCl buffer (pH 8.0) until no phospholipae B activity was detected in the soluble fraction. The enzyme was extracted with Triton X-100 from the final residue and purified about 1,390-fold by sequential chromatofocusing, Sepharose 6B, and DEAE-Sephadex A-50 column chromatography. The final preparation showed a single broad protein band on SDS-polyacrylamide gel electrophoresis when stained with silver stain reagent and PAS-reagent. The molecular weight of phospholipase B was about 390,000 and 140,000-190,000 as estimated by gel filtration on Sepharose 6B and SDS-polyacrylamide gel electrophoresis, respectively, suggesting that phospholipase B is an oligomeric protein. The isoelectric point was at pH 4.5. Phospholipase B has two pH optima, one acidic (pH 2.5-3.0) and the other alkaline (pH 7.2-8.0). At acidic pH the phospholipase B activity was greatly increased in the presence of divalent metal ions, although metal ions are not a factor for enzyme activity. On the other hand, at alkaline pH the enzyme required Ca2+ or Mn2+ for activity. The pH- and thermal-stabilities at both pHs were similar. The phospholipase B hydrolyzed all diacylphospholipids tested at acidic pH, but hydrolyzed only phosphatidylcholine at alkaline pH. The hydrolysis rates of lysophospholipids were much higher (about 10-fold) than those of diacylphospholipids at both pHs.

Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Publishing Authors By Initials

Y Kuwabara,M Maruyama,Y Watanabe,S Tanaka,M Takakuwa,Y Tamai,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 104

Page Numbers: 236-41

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1988

Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii. Information

Substance Name: Lysophospholipase

Registry Number: EC 3.1.1.5

Grant and Affiliation Information for Purification and some properties of membrane-bound phospholipase B from Torulaspora delbrueckii.

AFFILIATION: Department of Agricultural Chemistry, College of Agriculture, Ehime University.

Country: JAPAN

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MEDLINETA: J Biochem

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