000			01537nam a2200277Ia 4500
003			MX-MdCICY
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040			_cCICY
090			_aB-11140
245	1	0	_aPorcine pancreatic lipase. Completion of the primary structure
490	0		_vBiochimica et Biophysica Acta, 671(2), p.129-138, 1981
520	3		_aThe 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
650	1	4	_aLIPASE
650	1	4	_aPRIMARY STRUCTURE
650	1	4	_aPEPTIDE AGGREGATION
650	1	4	_a(PIG)
700	1	2	_aDe Caro, J.
700	1	2	_aBoudouard, M.
700	1	2	_aBonicel, J.
700	1	2	_aGuidoni, A.
700	1	2	_aDesnuelle, P.
700	1	2	_aRovery, M.
856	4	0	_uhttps://drive.google.com/file/d/1kvtxi5lBA2jT5OQHiKqZBvEziyv2UIcK/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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