| 1. |
- Breimer, Michael, 1951, et al.
(författare)
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Blood group glycosphingolipids of human kidney.
- 1983
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Ingår i: Glycoconjugates (eds Chester, A, Heinegård D, Lundblad A, Svensson S).. - Lund : Rham Publ Lund. ; , s. 421-422
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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| 2. |
- Erlanson-Albertsson, C, et al.
(författare)
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Importance of the N-terminal sequence in porcine pancreatic colipase
- 1981
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Ingår i: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002. ; 665:2, s. 5-250
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Tidskriftsartikel (refereegranskat)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 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.
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| 3. |
- Fex, G, et al.
(författare)
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Isolation and partial characterization of a low molecular weight trypsin inhibitor from human urine
- 1981
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Ingår i: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002 .- 0005-2795. ; 667:2, s. 8-303
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Tidskriftsartikel (refereegranskat)abstract
- A low molecular weight glycoprotein which completely inhibited trypsin at a 1 : 1 molar ratio was isolated from human urine. It was generated from a precursor molecule which in turn derived from plasma inter-alpha-trypsin inhibitor. It had one polypeptide chain with a molecular weight of about 20 000 and a high content of half-cystine residues. Its amino-terminal amino-acid sequence was Val-Thr-Glu-Val-Thr-X-Leu-Glu-Asp-.
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| 4. |
- Larsson, Anita, et al.
(författare)
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The identity and properties of two forms of activated colipase from porcine pancreas
- 1981
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Ingår i: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002. ; 664:3, s. 48-538
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Tidskriftsartikel (refereegranskat)abstract
- Colipase is excreted as a procolipase, colipase101. It is activated by low concentrations of trypsin, hydrolyzing the N-terminal pentapeptide. With higher concentrations of trypsin or in the presence of Ca2+ a smaller form of colipase containing 85 amino acids, appears. It has glycine as the N-terminal and arginine as the C-terminal amino acid residue and has lost 11 amino acids in the C-terminal chain. The ability of colipase85 to activate lipase with tributyrin as substrate is about the same as for colipase96 and procolipase. With fenfluramine, an anoretic agent, added to the tributyrin colipase assay system, the specific activities of colipase96 and colipase85 are similar and about five times higher than that of colipase101. With intralipid as substrate colipase85 enables lipase to reach the triacylglycerol substrate more rapidly than colipase96, having about six times shorter lagtime for a given concentration. Colipase84, obtained by splitting off the C-terminal arginine from colipase85, has a lagtime somewhere between colipase85 and colipase96, pointing to the importance of arginine85 for Intralipid activity. The binding between lipase and colipase has about the same strength for procolipase, colipase96 and for colipase85, Kd being about 10(-6) M either in buffer or in the presence of 2 mM taurodeoxycholate at pH 7. Addition of long chain fatty acids in the presence of bile salts increases the binding strength between colipase and lipase 100-fold, both for colipase96 and colipase85.
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| 5. |
- Larsson, C.G., et al.
(författare)
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Diffraction of UV excited photoelectrons by an ordered overlayer
- 1983
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Ingår i: Physica Scripta. - 0031-8949 .- 1402-4896. ; T4, s. 44-46
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Tidskriftsartikel (refereegranskat)abstract
- Angle resolved UV photoemission spectra obtained from Cu(111)-(√3 × √3)R30° Xe and Cu(111)-(√3 × √3)R30° CO samples are compared with spectra obtained from the clean substrate. Interest is focussed on the adsorbate induced changes in the Cu3d band range of initial energies. From the similarity between the spectra observed for the ordered Xe and CO overlayers we conclude that the changes are primarily due to diffraction of the photoexcited Cu3d electrons by the adsorbate. This is supported also by calculated photoelectron energy distributions.
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