Literature DB >> 6327565

Turkey muscle acylphosphatase: purification and comparative studies.

G Camici, G Manao, M Stefani, A Berti, G Cappugi, G Liguri, G Ramponi.   

Abstract

Turkey muscle acylphosphatase is strongly bound to anti-(horse muscle acylphosphatase ) antibodies covalently linked to an agarose resin. This permits use of an affinity chromatography step in the purification, which increased the final yield and allowed us to isolate three different molecular forms of the enzyme. Form 1 is a mixed disulfide between the polypeptide chain and glutathione; form 3 is an S-S dimer of the polypeptide chain present in form 1, while form 2, present in a very low amount, consists of a polypeptide chain quite similar in aminoacid composition to that found in form 1. The three molecular forms show very similar kinetic parameters. The comparison of these molecular forms with those isolated from horse muscle showed similar kinetic properties but different structural features.

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Year:  1984        PMID: 6327565

Source DB:  PubMed          Journal:  Ital J Biochem        ISSN: 0021-2938


  3 in total

1.  Rat muscle acylphosphatase: purification, amino sequence, and immunological characterization.

Authors:  A Berti; E Tremori; L Pazzagli; D Degl'Innocenti; G Camici; G Cappugi; G Manao; G Ramponi
Journal:  J Protein Chem       Date:  1991-02

2.  Purification and characterization of acylphosphatase erythrocyte isoenzyme from turkey muscle.

Authors:  M Stefani; D Degl'Innocenti; A Berti; G Cappugi; G Manao; G Camici; G Ramponi
Journal:  J Protein Chem       Date:  1990-10

3.  Guinea pig acylphosphatase: the amino acid sequence.

Authors:  G Manao; G Cappugi; A Modesti; M Stefani; R Marzocchini; D Degl'Innocenti; G Camici
Journal:  J Protein Chem       Date:  1988-08
  3 in total

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