Literature DB >> 6670355

[N-terminal sequence of a porphobilinogen synthase].

B Lingner, T Kleinschmidt.   

Abstract

The N-terminal sequence of porphobilinogen-synthase (EC 4.2.1.24) from bovine liver up to position 44 is given. After tryptic hydrolysis two N-terminal peptides with identical amino acid composition were isolated in the ratio 1:1. One peptide was blocked whereas the other one started with methionine and showed the same primary structure which had been estimated by automatic degradation of the enzyme. Four of the eight subunits of PBG-S have free methionine as N-terminal amino acid whereas the other half is blocked.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6670355     DOI: 10.1515/znc-1983-11-1229

Source DB:  PubMed          Journal:  Z Naturforsch C Biosci        ISSN: 0341-0382


  3 in total

1.  Isolation of a rat liver delta-aminolevulinate dehydrase (ALAD) cDNA clone: evidence for unequal ALAD gene dosage among inbred mouse strains.

Authors:  T R Bishop; P J Cohen; S H Boyer; A N Noyes; L P Frelin
Journal:  Proc Natl Acad Sci U S A       Date:  1986-08       Impact factor: 11.205

Review 2.  Porphobilinogen synthase, the first source of heme's asymmetry.

Authors:  E K Jaffe
Journal:  J Bioenerg Biomembr       Date:  1995-04       Impact factor: 2.945

3.  Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone.

Authors:  J G Wetmur; D F Bishop; C Cantelmo; R J Desnick
Journal:  Proc Natl Acad Sci U S A       Date:  1986-10       Impact factor: 11.205

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.