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Porcine pancreatic lipase. Completion of the primary structure

Tipo de material: TextoTextoSeries ; Biochimica et Biophysica Acta, 671(2), p.129-138, 1981Trabajos contenidos:
  • De Caro, J
  • Boudouard, M
  • Bonicel, J
  • Guidoni, A
  • Desnuelle, P
  • Rovery, M
Tema(s): Recursos en línea: Resumen: The complete primary structure of a lipase (trlacylglycerol hydrolase; EC 3.1.1.3)is presented for the first time. The porcine pancreatic enzyme which was investigated is composed of a single chain of 449 amino acids. Upon fragmentation by CNBr, five peptides were obtained. The sequence of four of them (CN I-CN IV)has already been published. The present report deals with the arrangement of the 142 amino acids of the C-terminal peptide CN V, thus completing the analysis of the whole molecule. Special problems resulting from incomplete cleavage of some peptide bonds in CN V and aggregation of large peptides were overcome using Sephadex filtration of succinylated derivatives in 50
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The complete primary structure of a lipase (trlacylglycerol hydrolase; EC 3.1.1.3)is presented for the first time. The porcine pancreatic enzyme which was investigated is composed of a single chain of 449 amino acids. Upon fragmentation by CNBr, five peptides were obtained. The sequence of four of them (CN I-CN IV)has already been published. The present report deals with the arrangement of the 142 amino acids of the C-terminal peptide CN V, thus completing the analysis of the whole molecule. Special problems resulting from incomplete cleavage of some peptide bonds in CN V and aggregation of large peptides were overcome using Sephadex filtration of succinylated derivatives in 50

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