Porcine pancreatic lipase. Completion of the primary structure 

 -  Biochimica et Biophysica Acta, 671(2), p.129-138, 1981 .
<br/><br/> 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 
<br/><br/><label>Subjects--Topical Terms: </label><br/>LIPASE<br/>PRIMARY STRUCTURE<br/>PEPTIDE AGGREGATION<br/>(PIG)