Literature DB >> 1095911

Structural aspects of the milk clotting process. Comparative features with the blood clotting process.

P Jollès.   

Abstract

The enzyme chymosin and its substrate, a casein fraction called k-casein, are involved in the milk clotting process. Recent data concerning the structure (peptide and sugar moieties) of various k-caseins and their role in casein micelles formation and stabilization are presented. The molecular events occurring during the primary phase of chymosin action on k-casein are discussed. Finally some structural features concerning more particularly the caseinoglycopeptides and the fibrinopeptides as well as the action of chymosin and thrombin involved in the milk and blood clotting processes are compared. Three examples of sequences of portions of k-caseins and fibrinogen presenting homology are presented.

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Year:  1975        PMID: 1095911     DOI: 10.1007/bf01792075

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  64 in total

1.  The primary structure of prochymosin (prorennin) EC 3.4.4.3. some tryptic fragments of a maleylated preparation.

Authors:  Bent Foltmann; Bente Andersen
Journal:  FEBS Lett       Date:  1971-09-15       Impact factor: 4.124

2.  AMINO-ACID SEQUENCE INVESTIGATIONS OF FIBRINOPEPTIDES FROM VARIOUS MAMMALS: EVOLUTIONARY IMPLICATIONS.

Authors:  R F DOOLITTLE; B BLOMBAECK
Journal:  Nature       Date:  1964-04-11       Impact factor: 49.962

3.  The role of the carbohydrate moiety in bovine fibrinogen.

Authors:  K LAKI; L MESTER
Journal:  Biochim Biophys Acta       Date:  1962-02-12

Review 4.  Structural aspects of the fibrinogen to fibrin conversion.

Authors:  R F Doolittle
Journal:  Adv Protein Chem       Date:  1973

5.  Localisation of carbohydrate in the subunits of human fibinogen and its plasmin induced fragments.

Authors:  P J Gaffney
Journal:  Biochim Biophys Acta       Date:  1972-04-15

6.  The effect of plasmin on the subunit structure of human fibrinogen.

Authors:  S V Pizzo; M L Schwartz; R L Hill; P A McKee
Journal:  J Biol Chem       Date:  1972-02-10       Impact factor: 5.157

7.  The chromatographic purification of human kappa-casein.

Authors:  C Alais; P Jollès
Journal:  J Chromatogr       Date:  1969-11-11

8.  Fractionation of S-carboxymethyl-kappa-casein and characterization of the components.

Authors:  A G Mackinlay; R G Wake
Journal:  Biochim Biophys Acta       Date:  1965-06-15

9.  Present knowledge concerning the amino-acid sequence of cow kappa-casein.

Authors:  J Jollès; P Jollès; C Alais
Journal:  Nature       Date:  1969-05-17       Impact factor: 49.962

10.  Amphiphile nature of k-casein as the basis for its micelle stabilizing property.

Authors:  R J Hill; R G Wake
Journal:  Nature       Date:  1969-02-15       Impact factor: 49.962

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  5 in total

1.  Characterization of kappa-casein and keratin domains in fibrinogen.

Authors:  P Jollés; J Jollés; A Henschen
Journal:  J Mol Evol       Date:  1981       Impact factor: 2.395

2.  Development and validation of models for the investigation of blood clotting in idealized stenoses and cerebral aneurysms.

Authors:  Andrew Narracott; Stephen Smith; Patricia Lawford; Hao Liu; Ryutaro Himeno; Iain Wilkinson; Paul Griffiths; Rodney Hose
Journal:  J Artif Organs       Date:  2005       Impact factor: 1.731

3.  Prediction of the conformation of the cow and sheep kappa-caseins.

Authors:  M H Loucheux-Lefebvre; J P Aubert; P Jollès
Journal:  Biophys J       Date:  1978-09       Impact factor: 4.033

4.  Structural relatedness of kappa-casein and fibrinogen gamma-chain.

Authors:  P Jollès; M H Loucheux-Lefebvre; A Henschen
Journal:  J Mol Evol       Date:  1978-10-06       Impact factor: 2.395

5.  Characterization of the amino acids of bovine fibrinogen involved in the fibrinogen-thrombin interaction of the blood clotting process. Comparison with the milk clotting process.

Authors:  N M Kaye; P Jollès
Journal:  Mol Cell Biochem       Date:  1978-08-16       Impact factor: 3.396

  5 in total

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