The primary structure of porcine colipase II. I. The amino acid sequence

Charles, M.; Erlanson, Charlotte; Bianchetta, J.; Joffre, Jérémie; Guidoni, A.; Rovery, M.

doi:10.1016/0005-2795(74)90142-1

Cited by 83 publications

(18 citation statements)

References 9 publications

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“…However, it must be realized that these considerations only apply to the very slight degradations reported in this work. More extensive cleavages like those leading to the loss of a number of N-terminal and C-terminal residues in porcine colipase I1 [9] are probably due to several enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…Maylie et al [S] isolated two forms of porcine colipase. One, colipase I1 with 84 residues, has been fully sequenced [9] while the other (colipase I) has been reported to be longer by about 10 residues. Both were characterized by an N-terminal Gly-(Ile), sequence so that the 10 residues missing in colipase I1 could be assumed to be located on the carboxyl side of colipase I.…”

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confidence: 99%

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Stabilization of the C-Terminal Part of Pig and Horse Colipase by Carboxypeptidase and Trypsin Inhibitors

Chapus

Desnuelle

Foglizzo

2005

European Journal of Biochemistry

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Pig and horse colipases have been purified by a common procedure using trypsin and carboxypeptidase inhibitors as stabilizers. Two forms of pig colipase were identified : a predominant A1 form with about 103 -105 residues, and a minor slightly degraded A2 form in which the last two C-terminal residues, Asp and Ser, were lacking. This type of degradation is considerably slowed down by carboxypeptidase inhibitors. A total of four forms of the horse cofactor were characterized: two (A1 and Bl) were probably isocolipases which differed by only a few substitutions. Both contained the same number of residues (about 96), an N-terminal valine and an Arg-Ser-Glu-(Glx),,,-Arg C-terminal sequence. A2 and B2 were slightly degraded forms probably resulting from tryptic cleavage of the Arg-Ser bond in the above sequence. The presence of methionine in the horse cofactor allowed fragmentation by cyanogen bromide. The C-terminal fragment was composed of 16 or 17 residues and contained no histidine. The single histidine of horse B1 was found in the intermediary fragment between Met-I8 and Met-(n-16) or Met-(n-17). These data show that the Cterminal parts of both pig and horse colipases are still more exposed to proteolytic degradations than the N-terminal parts. Preliminary attempts to crystallize B1 were carried out.Pancreatic colipase is a small protein which acts as a cofactor for lipase during intraluminar digestion of dietary triglycerides in the presence of bile salts [I -31. It is now generally accepted that lipase alone cannot adsorb in vivo to bile-salt-coated triglyceride interfaces and that it must be anchored by the cofactor [4]. Colipase also protects lipase against interfacial denaturation [5 -71. It is clear that these effects require specific protein-lipid and protein-protein interactions which will only be understood after elucidation of the tridimensional structure of the colipase molecule.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Stabilization of the C-Terminal Part of Pig and Horse Colipase by Carboxypeptidase and Trypsin Inhibitors

Chapus

Desnuelle

Foglizzo

2005

European Journal of Biochemistry

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“…The protein was reduced and carboxymethylated [18] prior to Edman degradation which was carried out on an Applied Biosystems sequencer Model 470 A, and phenylthiohydantoin (PTH) identification by means of an Applied PTH column (5/zm, 2.1 x 220 mm).…”

Section: Amino Acid Analysis and Automated Edman Degradationmentioning

confidence: 99%

Purification and some characteristics of chicken liver L‐2‐hydroxyacid oxidase A

Dupuis¹,

Caro²,

Brachet³

et al. 1990

FEBS Letters

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The isozyme A of L-2-hydroxyacid oxidase is a peroxisomal flavoenzyme that catalyzes the oxidation of short-chain aliphatic L-2-hydroxyacids in many tissues of higher organisms. A new purification procedure allowed us to obtain a 1400-fold purified enzyme from chicken liver. The Nterminal amino acid of the polypeptide chain was found to be blocked as that of spinach glycolate oxidase, contrastingly with that of rat kidney isozyme B. Its amino acid composition was comparable to that of other known L-2-hydroxyacid oxidases. Despite different substrate specificity, some immunological identity was observed between chicken liver L-2-hydroxyacid isozyme A and rat kidney isozyme B.

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“…A general interpretation of the colipase II spectrum has already been reported [7]. Colipase II is one of the two major forms of the cofactor isolated in [8] ; its covalent structure (84 residues) has been fully elucidated [9,10] and corresponds to a compact central core crosslinked by 5 disulfide bridges with two terminal tails. Two other forms of the cofactor have been obtained [11,12] and some characteristics of 3 aromatic residues of a 106 residue long form of colipase have been investigated by NMR spectroscopy [ 13 ].…”

Section: Introductionmentioning

confidence: 99%