Literature DB >> 6100723

Human skeletal muscle acylphosphatase: the primary structure.

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

Abstract

Human skeletal muscle acylphosphatase, purified by a technique based on affinity chromatography on immunoadsorbent, has been sequenced completely using tryptic and peptic peptide series, prepared by reverse-phase high-pressure liquid chromatography. The sequence analysis was carried out on all the isolated tryptic peptides using a manual Edman degradation technique and time-course analysis of the released amino acids by carboxypeptidase A. The enzyme is NH2-blocked and the blocking group has been identified by fast atom bombardment mass spectrometry.

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Year:  1984        PMID: 6100723

Source DB:  PubMed          Journal:  Mol Biol Med        ISSN: 0735-1313


  4 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.  Properties of Cys21-mutated muscle acylphosphatases.

Authors:  A Modesti; N Taddei; F Chiti; M Bucciantini; F Magherini; S Rigacci; M Stefani; G Raugei; G Ramponi
Journal:  J Protein Chem       Date:  1996-01

3.  Bovine testis acylphosphatase: purification and amino acid sequence.

Authors:  L Pazzagli; G Cappugi; G Camici; G Manao; G Ramponi
Journal:  J Protein Chem       Date:  1993-10

4.  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
  4 in total

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