PURIFICATION AND PROPERTIES OF 2 PHOSPHOLIPASES-D FROM STREPTOMYCES SP

被引：73

作者：

CARREA, G

DARRIGO, P

PIERGIANNI, V

RONCAGLIO, S

SECUNDO, F

SERVI, S

机构：

[1] POLITECN MILAN,CNR,CTR STUDIO SOSTANZE ORGAN NAT,DIPARTIMENTO CHIM,I-20131 MILAN,ITALY

[2] CNR,IST CHIM ORMONI,I-20131 MILAN,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM | 1995年 / 1255卷 / 03期

关键词：

PHOSPHOLIPASE D; PHOSPHOLIPID; TRANSPHOSPHATIDYLATION; MALDI-MS; STREPTOMYCES;

D O I：

10.1016/0005-2760(94)00241-P

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two enzymes with phospholipase D activity were purified from Streptomyces strains (PMF and PM43) by column chromatography on Fractogel TSK CM-650(S), Sephadex G-100 and Fractogel EMD DEAE-650(M). The purified preparations were found to be homogeneous by SDS-PAGE, capillary electrophoresis and analytical gel filtration. The molecular masses, assessed by MALDI-MS spectrometry, were 53.864 kDa for PMF and 54.147 kDa for PM43. The isoelectric point was 9.1 for both enzymes. The enzymes were most active at around 60 degrees C and stable between pH 3 and 9 and below 50 degrees C. The pH optima were between 4 and 6 for PMF and between 6 and 7 for PM43. Both phospholipases displayed high transphosphatidylation activity but PMF was more selective than PM43.

引用

页码：273 / 279

页数：7

共 24 条

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