Low-molecular-weight secretory phospholipases A 2 (sPLA 2 s) are a subgroup of PLA 2 s, which are secreted, bind to receptors, and may act as intercellular signaling modulators. At least 10 different groups have been characterized in mammals, and there is expanding evidence of the significance of sP
Multiple forms of porcine pancreatic phospholipase A2: Isolation and specificity
✍ Scribed by Tsao, Francis H. C. ;Cohen, Herschel ;Snyder, William R. ;Kézdy, Ferenc J. ;Law, John H.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 420 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0091-7419
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✦ Synopsis
Abstract
Porcine pancreatic phospholipase A~2~ was purified from commercial pancreatin by a method involving heat denaturation, trichloroacetic acid precipitation, and DEAE‐cellulose chromatography. Assaying the eluate of the chromatography step by a new titrimetric method using vegetable lecithin‐albumin emulsion as the substrate, several species of phospholipase A were found. Some of these went undetected when the conventional egg yolk emulsion assay was used. Two phospholipases A~2~ were isolated in a homogeneous form and shown to have similar chemical and physical properties. Catalytic specificity of the two enzymes differs remarkably toward lecithins in different emulsified states.
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