caa a22 4500 397558317 CHVBK 20180308164809.0 cr unu---uuuuu 161202e199603 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021279 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021279 Purification and Properties of Rat Liver Peroxisomal Very-Long-Chain Acyl-CoA Synthetase [Elektronische Daten] [Yasushi Uchida, Naomi Kondo, Tadao Orii, Takashi Hashimoto] It is generally accepted that there are two different acyl-CoA synthetases in rat liver peroxisomes. One is long-chain acyl-CoA synthetase, and the other very-long-chain acyl-CoA synthetase. Nowadays, the nature of long-chain acyl-CoA synthetase is well-known, but that of very-long-chain acyl-CoA synthetase remains unclear. Very-long-chain acyl-CoA synthetase has been extracted from the washed membrane fraction of frozen rat liver peroxisomes with a buffer containing a detergent, and has been purified by chromato-graphy on Ultrogel Ac A 34, calcium phosphate gel/cellulose, blue dextran-Sepharose 4B and DEAE-Toyopearl. The molecular masses of the native enzyme and the subunit were estimated to be 235 and 70 kDa, respectively. This enzyme showed marked differences in behavior from long-chain acyl-CoA synthetase during purification. The carbon chain length specificity of very-long-chain acyl-CoA synthetase differed from that of long-chain acyl-CoA synthetase. Very-long-chain acyl-CoA synthetase was active toward long- and very-long-chain fatty acids, but more active toward very-long-chain fatty acids compared with long-chain acyl-CoA synthetase. Antibodies against long-chain acyl-CoA synthetase did not cross-react to very-long-chain acyl-CoA synthetase. Based on these data, the final enzyme preparation is judged to be highly purified very-long-chain acyl-CoA synthetase from rat liver peroxisomes. © by the Journal of Biochemistry Regular Papers nationallicence adrenoleukodystrophy nationallicence long-chain acyl-CoA synthetase nationallicence peroxisome nationallicence purification nationallicence very-long-chain acyl-CoA synthetase nationallicence Uchida Yasushi Department of Pediatrics, Gifu University School of Medicine Gifu, Gifu 500 aut Kondo Naomi Department of Pediatrics, Gifu University School of Medicine Gifu, Gifu 500 aut Orii Tadao Department of Pediatrics, Gifu University School of Medicine Gifu, Gifu 500 aut Hashimoto Takashi Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut The Journal of Biochemistry Oxford University Press 119/3(1996-03), 565-571 0021-924X 119:3<565 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021279 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021279 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Uchida Yasushi Department of Pediatrics, Gifu University School of Medicine Gifu, Gifu 500 aut NATIONALLICENCE 700 1- Kondo Naomi Department of Pediatrics, Gifu University School of Medicine Gifu, Gifu 500 aut NATIONALLICENCE 700 1- Orii Tadao Department of Pediatrics, Gifu University School of Medicine Gifu, Gifu 500 aut NATIONALLICENCE 700 1- Hashimoto Takashi Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/3(1996-03), 565-571 0021-924X 119:3<565 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford