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Purification of rabbit platelet secretory phospholipase A2 and its characteristics.

Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Research Abstract Details 

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  • Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Abstract Text:

    h mizushimaH Mizushima,i kudoI Kudo,k horigomeK Horigome,m murakamiM Murakami,m hayakawaM Hayakawa,d k kimD K Kim,e kondoE Kondo,m tomitaM Tomita,k inoueK Inoue,

    It was reported previously that rat platelets release phospholipase A2 upon in vitro stimulation by thrombin, ADP, or A23187 (Horigome, K., Hayakawa, M., Inoue, K., & Nojima, S. (1987) J. Biochem. 101, 53-61). Secretion of phospholipase A2 was also observed with rabbit platelets. Rabbit platelets seem to release phospholipase A2 upon stimulation in vivo, because the rabbit plasma taken immediately after intravenous injection of PAF contained an appreciable level of phospholipase A2 activity and fewer platelets. Rabbit platelet phospholipase A2 released in vitro was purified by column chromatography using Sepharose CL-4B conjugated with anti-rat platelet derived phospholipase A2 monoclonal antibody, followed by reversed-phase HPLC. The purified enzyme was subjected to structural analysis by HPLC peptide mapping and primary sequence determination of the separated peptides. Based on the homology with rat platelet secretory phospholipase A2 (Hayakawa, M., Kudo, I., Tomita, M., Nojima, S., & Inoue, K. (1988) J. Biochem. 104, 767-772), a partial primary structure (62 amino acid residues) of the rabbit enzyme was tentatively determined; the two sequences were highly homologous (72%). The rabbit sequence was also nearly identical to that of rabbit ascitic fluid phospholipase A2, which was determined by Forst et al. (Forst, S., Weiss, J., Elsbach, P., Maraganore, J.M., Reardon, I., & Heinrikson, R.L. (1986) Biochemistry 25, 8381-8385). Phospholipase A2 from the membrane fraction of rabbit platelets was also purified; it had the same characteristics and th same amino-terminal sequence as the purified secretory enzyme. Secretory and membrane-bound phospholipase A2 of rabbit platelets may in fact be identical.(ABSTRACT TRUNCATED AT 250 WORDS)

    Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Publishing Authors By Initials

    h mizushimaH Mizushima,i kudoI Kudo,k horigomeK Horigome,m murakamiM Murakami,m hayakawaM Hayakawa,dk kimDK Kim,e kondoE Kondo,m tomitaM Tomita,k inoueK Inoue,

    For similar animals: chordata: vertebrates: mammals: lagomorpha: rabbits research abstracts see: animals: chordata: vertebrates: mammals: lagomorpha: rabbits research

    PUBMED ID PMID:

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    Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 105

    Page Numbers: 520-5

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Apr

    YEAR: 1989

    Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Keywords Mesh Terms:

    KEYWORDS: Rabbits

    MESH TERMS: drug effects

    Chemical & Substance for Abstract: Purification of rabbit platelet secretory phospholipase A2 and its characteristics. Information

    Substance Name: Phospholipases A2

    Registry Number: EC 3.1.1.4

    Grant and Affiliation Information for Purification of rabbit platelet secretory phospholipase A2 and its characteristics.

    AFFILIATION: Faculty of Pharmaceutical Sciences, University of Tokyo.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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