Chemical modification of pancreatic lipase Effect on the colipase‐reactivated and the ‘true’ lipase activity

Erlanson, Charlotte

doi:10.1016/0014-5793(77)81061-2

Cited by 21 publications

(5 citation statements)

References 15 publications

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“…Attempts to identify specific amino acid residues of colipase essential for activity were first made by studying the properties of chemically modified proteins (Erlanson, 1977;Erlanson et al, 1977;Erlanson-Albertsson, 1980;De Car0 et al, 1983) and by using biophysical methods including ultraviolet spectrophotometry, fluorescence spectrometry and 'H-NMR (Sari et al, 1975(Sari et al, , 1978Canioni et al, 1979Canioni et al, , 1980Canioni and Cozzone, 1979a,b;Cozzone, 1976;Cozzone et al, 1981;Granon, 1986;Granon et al, 1981;McIntyre et al, 1987;Wieloch and Falk, 1978;Wieloch et al, 1979). NMR studies on procolipase and its trypsin-treated derivative included pH titration of the proteins, determination of pK values of ionizable groups and identification and preliminary sequential assignment of aromatic sidechain protons.…”

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confidence: 99%

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two-Dimensional and Three-Dimensional NMR

Breg¹,

Sarda²,

Cozzone³

et al. 1995

Eur J Biochem

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Procolipase is the precursor of colipase, which acts as protein cofactor for the activity of pancreatic lipase. The solution structure of procolipase has been determined by 1H NMR using two- and three-dimensional measurements. The secondary structure determination identified two separate three-stranded beta-sheet regions with concomitant hydrogen bond patterns. The tertiary structure of the protein was determined using 863 non-trivial proton--proton distance constraints, 14 hydrogen bond distance constraints and 55 phi and 25 X1 dihedral constraints. The structure that was obtained from distance geometry and energy refinement contains three highly disordered loops as well as a disordered N- and C-terminal region. The remaining part of the structure is well defined with a root-mean-square deviation (rmsd) relative to the average of 0.09 +/- 0.02 nm for backbone atoms (residues 11-30, 37-50, 57-69, 83-89). The protein comprises two identical domains, each containing a three-strand beta-sheet and two disulfide bonds: a 15-residue region in each domain superimposes with 0.07 nm rmsd, measured on backbone atoms. The solution structure is nearly identical to the crystal structure. It is in agreement with previous NMR data and, in combination with these data, supports the current model of procolipase micelle interaction and the lipase activation by colipase.

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confidence: 99%

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two-Dimensional and Three-Dimensional NMR

Breg¹,

Sarda²,

Cozzone³

et al. 1995

Eur J Biochem

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“…Most of the information on the specific contribution of particular residues of the protein to its biological function was obtained from kinetic and binding studies performed with native and chemically modified colipase (15)(16)(17)(18)(19)(20)(21) and by using a variety of biophysical techniques including ultraviolet spectroscopy (22,23), spectrofluorometry (24)(25)(26), circular dichroism (13,14), NMR (27)(28)(29)(30)(31)(32)(33) and photo-CIDNP (34). From these studies it was concluded that the hydrophobic peptide segments at positions 6 to 9 and 53 to 59, which are highly conserved in the homologous proteins, are involved in the binding of colipase to interface.…”

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confidence: 99%

“…There is evidence from physicochemical studies that two of these residues (Tyr,, and Tyr,,) are located on the surface of the protein (5,25,31,32). On the other hand, it was proposed, from studies on the binding and activating properties of colipase modified by carbodiimide, that at least one of the carboxyls of residue Glu,, and Asp,,, conserved in all proteins, might contribute to the stabilization of the colipase-lipase complex through ionic bonding (15,16). 31, 32).…”

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confidence: 99%

“…However, it was not definitely established which of the two histidines of the porcine protein (His,,, or His,,) was involved in this interaction (25,28,32). On the other hand, it was proposed, from studies on the binding and activating properties of colipase modified by carbodiimide, that at least one of the carboxyls of residue Glu,, and Asp,,, conserved in all proteins, might contribute to the stabilization of the colipase-lipase complex through ionic bonding (15,16). Recently, polyclonal and monoclonal antibodies (35, 36) have also been used to probe the functional domains of colipase in spatial relationship with the antigenic regions of the protein.…”

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Conformational prediction studies on pancreatic colipase

Bellon

Dezan

Rugani

et al. 1991

International Journal of Peptide and Protein Research

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Comparison of the primary structures of pancreatic colipases from man, pig, horse and rat shows a high degree of homology between proteins. Fifty-two out of the 95 residues of the polypeptide are identical. All colipases contain 10 half-cystines which are located at invariant positions. The secondary structure of colipases has been predicted from the sequence using the statistical method of Chou and Fasman and the method of Gibrat, Gamier and Robson based on information theory. Predictions indicate that colipases have a low content of %-helix and ,&strand structure. The two segments at positions 7-10 and 56-59. assumed to be part of the lipid binding domain, have predicted ,&sheet conformation and should be in close spatial vicinity to each other in the proteins. Four fl-turns are predicted in all colipases at positions 3-6. 46-49, 61-64. and 81-84. They might contribute, with the five disulfide bridges, to a tight packing of the protein molecule. Surface residues and major sequential antigenic determinants of mammalian colipases have been predicted using methods based either on hydrophilicity/hydropathy scales or amino acid mutability. From these studies, it appears that colipases exhibit large conformational homologies. In the absence of data on the tertiary structure of colipase, predictive methods, together with physico-chemical and immunological studies, provide valuable information on the conformation of the protein in relation to the topology of residues involved in the functional and antigenic sites. K(,I. i i~o r d~: antigenic determinants; colipase; conformational homology: pancreas: prediction: secondary structure: sequence homology

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Solution Structure of Porcine Pancreatic Procolipase as Determined from ¹H Homonuclear Two‐Dimensional and Three‐Dimensional NMR

Breg

Sarda²,

Cozzone

et al. 1995

European Journal of Biochemistry

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Procolipase is the precursor of colipase, which acts as protein cofactor for the activity of pancreatic lipase. The solution structure of procolipase has been determined by 1H NMR using two‐ and three‐dimensional measurements. The secondary structure determination identified two separate three‐stranded β‐sheet regions with concomitant hydrogen bond patterns. The tertiary structure of the protein was determined using 863 non‐trivial proton–proton distance constraints, 14 hydrogen bond distance constraints and 55 Ø and 25 χ1 dihedral constraints. The structure that was obtained from distance geometry and energy refinement contains three highly disordered loops as well as a disordered N‐ and C‐terminal region. The remaining part of the structure is well defined with a root‐mean‐square deviation (rmsd) relative to the average of 0.09±0.02 nm for backbone atoms (residues 11–30, 37–50, 57–69, 83–89). The protein comprises two identical domains, each containing a three‐strand β‐sheet and two disulfide bonds: a 15‐residue region in each domain superimposes with 0.07 nm rmsd, measured on backbone atoms. The solution structure is nearly identical to the crystal structure. It is in agreement with previous NMR data and, in combination with these data, supports the current model of procolipase micelle interaction and the lipase activation by colipase.

show abstract

Chemical modification of pancreatic lipase Effect on the colipase‐reactivated and the ‘true’ lipase activity

Cited by 21 publications

References 15 publications

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two-Dimensional and Three-Dimensional NMR

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two-Dimensional and Three-Dimensional NMR

Conformational prediction studies on pancreatic colipase

Solution Structure of Porcine Pancreatic Procolipase as Determined from ¹H Homonuclear Two‐Dimensional and Three‐Dimensional NMR

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Chemical modification of pancreatic lipase Effect on the colipase‐reactivated and the ‘true’ lipase activity

Cited by 21 publications

References 15 publications

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two-Dimensional and Three-Dimensional NMR

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two-Dimensional and Three-Dimensional NMR

Conformational prediction studies on pancreatic colipase

Solution Structure of Porcine Pancreatic Procolipase as Determined from 1H Homonuclear Two‐Dimensional and Three‐Dimensional NMR

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Solution Structure of Porcine Pancreatic Procolipase as Determined from ¹H Homonuclear Two‐Dimensional and Three‐Dimensional NMR