Literature DB >> 6172357

[Human embryonic haemoglobins. Ac-Ser-Leu-Thr-is the N-terminal sequence of the zeta-chains (author's transl)].

H Aschauer, W Schäfer, T Sanguansermsri, G Braunitzer.   

Abstract

The complete amino acid sequence of the embryonic zeta-chains has been reported in an earlier communication (Aschauer, H., Sanguansermsri, T. & Braunitzer, G. (1981), Hoppe-Seyler's Z. Physiol. Chem. 362, 1159-1162). To elucidate the nature of the N-terminal blocking group, tryptical cleavage of the zeta-chains was carried out and the N-terminal tryptic tetrapeptide was isolated by high performance liquid chromatography on reversed phase (RP 8). The tetrapeptide was digested with pronase and the mixture was subjected to mass spectrometry by chemical ionization. By this method Ac-Ser was found to be the N-terminus. In a second experiment the tetrapeptide was permethylated and analysed by mass spectrometry with electron ionization. The N-terminal sequence was found to be Ac-Ser-Leu-Thr-.

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Year:  1981        PMID: 6172357

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  3 in total

1.  Universal regularities in protein primary structure: preference in bonding and periodicity.

Authors:  O C Ivanov; B Förtsch
Journal:  Orig Life Evol Biosph       Date:  1986       Impact factor: 1.950

2.  Some effects of post-translational N-terminal acetylation of the human embryonic zeta globin protein.

Authors:  A Scheepens; R Mould; O Hofmann; T Brittain
Journal:  Biochem J       Date:  1995-09-01       Impact factor: 3.857

3.  Allosteric modulation of oxygen binding to the three human embryonic haemoglobins.

Authors:  O Hofmann; R Mould; T Brittain
Journal:  Biochem J       Date:  1995-03-01       Impact factor: 3.857

  3 in total

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