Importance of the N-terminal sequence in porcine pancreatic colipase
(1981) In Biochimica et Biophysica Acta 665(2). p.5-250- Abstract
Colipase exists in pancreatic juice in a pro-form which is activated by limited trypsin hydrolysis. During this activation, the N-terminal pentapeptide 1Val-Pro-Asp-Pro-5Arg is cleaved. The new N-terminal sequence formed, 6Gly-Ile-Ile-Ile-10Asn, contains three isoleucine residues. The importance of these for stimulating lipase activity has been investigated by successive Edman degradation of epsilon-acetimidolysine residues followed by limited trypsin hydrolysis. The epsilon-amidinated colipase obtained was fully active both with a phospholipid-covered triacylglycerol (Intralipid) and tributyrin as substrate. After removal of the three isoleucine residues, the activity of colipase was lost with Intralipid but not with tributyrin as... (More)
Colipase exists in pancreatic juice in a pro-form which is activated by limited trypsin hydrolysis. During this activation, the N-terminal pentapeptide 1Val-Pro-Asp-Pro-5Arg is cleaved. The new N-terminal sequence formed, 6Gly-Ile-Ile-Ile-10Asn, contains three isoleucine residues. The importance of these for stimulating lipase activity has been investigated by successive Edman degradation of epsilon-acetimidolysine residues followed by limited trypsin hydrolysis. The epsilon-amidinated colipase obtained was fully active both with a phospholipid-covered triacylglycerol (Intralipid) and tributyrin as substrate. After removal of the three isoleucine residues, the activity of colipase was lost with Intralipid but not with tributyrin as substrate. The shortened colipases regained their Intralipid activity upon addition of long-chain fatty acids. The binding of colipase to lipase was not affected by removal of the isoleucine residues.
(Less)
- author
- Erlanson-Albertsson, C LU and Larsson, A
- organization
- publishing date
- 1981-08-24
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Amino Acid Sequence, Animals, Colipases/pharmacology, Lipase/metabolism, Pancreas/analysis, Peptide Fragments/analysis, Protein Binding, Proteins/pharmacology, Swine, Trypsin
- in
- Biochimica et Biophysica Acta
- volume
- 665
- issue
- 2
- pages
- 5 - 250
- publisher
- Elsevier
- external identifiers
-
- pmid:7284423
- scopus:0019887467
- ISSN
- 0006-3002
- DOI
- 10.1016/0005-2760(81)90009-6
- language
- English
- LU publication?
- yes
- id
- 7d183236-90c0-4e2a-a653-e1967e45d380
- date added to LUP
- 2019-01-31 14:56:14
- date last changed
- 2023-12-31 20:32:51
@article{7d183236-90c0-4e2a-a653-e1967e45d380,
abstract = {{<p>Colipase exists in pancreatic juice in a pro-form which is activated by limited trypsin hydrolysis. During this activation, the N-terminal pentapeptide 1Val-Pro-Asp-Pro-5Arg is cleaved. The new N-terminal sequence formed, 6Gly-Ile-Ile-Ile-10Asn, contains three isoleucine residues. The importance of these for stimulating lipase activity has been investigated by successive Edman degradation of epsilon-acetimidolysine residues followed by limited trypsin hydrolysis. The epsilon-amidinated colipase obtained was fully active both with a phospholipid-covered triacylglycerol (Intralipid) and tributyrin as substrate. After removal of the three isoleucine residues, the activity of colipase was lost with Intralipid but not with tributyrin as substrate. The shortened colipases regained their Intralipid activity upon addition of long-chain fatty acids. The binding of colipase to lipase was not affected by removal of the isoleucine residues.</p>}},
author = {{Erlanson-Albertsson, C and Larsson, A}},
issn = {{0006-3002}},
keywords = {{Amino Acid Sequence; Animals; Colipases/pharmacology; Lipase/metabolism; Pancreas/analysis; Peptide Fragments/analysis; Protein Binding; Proteins/pharmacology; Swine; Trypsin}},
language = {{eng}},
month = {{08}},
number = {{2}},
pages = {{5--250}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Importance of the N-terminal sequence in porcine pancreatic colipase}},
url = {{http://dx.doi.org/10.1016/0005-2760(81)90009-6}},
doi = {{10.1016/0005-2760(81)90009-6}},
volume = {{665}},
year = {{1981}},
}