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European journal of biochemistry1982; 123(2); 347-354; doi: 10.1111/j.1432-1033.1982.tb19774.x

Pancreatic colipase: crystallographic and biochemical aspects.

Abstract: A detailed study of the crystallization of hog and horse colipases has been undertaken. Several crystallographic varieties have been obtained and a 0.3-nm resolution structure determination is actually in progress. The sequence of the A form of horse colipase (one methionine) is given. From spectrophotometric experiments and sequence comparisons, the involvement of the aromatic residue in position 52 in the micelle binding site has been demonstrated.
Publication Date: 1982-04-01 PubMed ID: 7075593DOI: 10.1111/j.1432-1033.1982.tb19774.xGoogle Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research provides insight into the crystallization of hog and horse colipases. This includes a study on their crystallographic varieties, resolution structure determination, and sequence comparisons, with a focus on the role of an aromatic residue at position 52 in micelle binding.

Crystallization of Hog and Horse Colipases

  • The research looked into the detailed process of crystallization of colipases sourced from hogs and horses. Crystallization is a process often used in structural biology to determine the arrangement of atoms within a substance.

Crystallographic Varieties

  • Different crystallographic varieties were obtained throughout the study. These varieties can help uncover different characteristics or traits of the substance, including its chemical composition and structure.

Resolution Structure Determination

  • A 0.3-nm resolution structure determination is underway. This process precisely measures the arrangement of atoms within the samples of hog and horse colipases.

Sequence of Horse Colipase

  • The sequence of the A form of horse colipase was established during the study. This sequence information can be critical in understanding the function and binding properties of the molecule.

Spectrophotometric Experiments and Sequence Comparisons

  • Spectrophotometric experiments and sequence comparisons were utilized to study the colipases. Spectrophotometry is a technique used to measure and analyze the light spectrum, providing qualitative and quantitative data about a substance.
  • The researchers applied this method to learn more about the colipase’s structural characteristics and interactions with other substances.

Involvement of Aromatic Residue

  • One of the significant findings of the study was the identification of the role of an aromatic residue located at position 52 in the micelle binding site on the colipase.
  • This aromatic residue appears to be crucial in facilitating the colipase’s binding with micelle, which is an aggregation of molecules in a colloidal solution. Understanding this interaction contributes to the knowledge of the colipase’s function and mechanism of action.

Cite This Article

APA
Pierrot M, Astier JP, Astier M, Charles M, Drenth J. (1982). Pancreatic colipase: crystallographic and biochemical aspects. Eur J Biochem, 123(2), 347-354. https://doi.org/10.1111/j.1432-1033.1982.tb19774.x

Publication

ISSN: 0014-2956
NlmUniqueID: 0107600
Country: England
Language: English
Volume: 123
Issue: 2
Pages: 347-354

Researcher Affiliations

Pierrot, M
    Astier, J P
      Astier, M
        Charles, M
          Drenth, J

            MeSH Terms

            • Amino Acid Sequence
            • Animals
            • Binding Sites
            • Colipases
            • Crystallization
            • Horses
            • Methods
            • Micelles
            • Pancreas / enzymology
            • Proteins
            • Spectrophotometry, Ultraviolet
            • Swine

            Citations

            This article has been cited 1 times.
            1. Kirschenbaum DM. Molar absorptivity and A 1% 1cm values for proteins at selected wavelengths of the visible and ultraviolet regions. XXIII. Appl Biochem Biotechnol 1984 Apr;9(2):187-206.
              doi: 10.1007/BF02798752pubmed: 6476824google scholar: lookup