Literature DB >> 2401356

Isolation and functional expression of pituitary peptidylglycine alpha-amidating enzyme mRNA. A variant lacking the transmembrane domain.

I Kato1, H Yonekura, H Yamamoto, H Okamoto.   

Abstract

We demonstrate that, in rat pituitary, peptidylglycine alpha-amidating enzyme was encoded by at least 5 distinct mRNAs. Southern blot and ribonuclease protection analyses revealed that the mRNAs arose through alternative splicing. A variant lacking the transmembrane domain-coding sequence was a major mRNA species for the enzyme in the pituitary. When the cDNAs were expressed in COS-7 cells, the variant was the most efficient in producing a secretory form (37 kDA) of the enzyme.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 2401356     DOI: 10.1016/0014-5793(90)81184-p

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1991-09-25       Impact factor: 16.971

2.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1991-08-25       Impact factor: 16.971

3.  A deletion polymorphism in the human alpha-2-macroglobulin (A2M) gene.

Authors:  G Matthijs; P Marynen
Journal:  Nucleic Acids Res       Date:  1991-09-25       Impact factor: 16.971

Review 4.  Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains.

Authors:  B A Eipper; S L Milgram; E J Husten; H Y Yun; R E Mains
Journal:  Protein Sci       Date:  1993-04       Impact factor: 6.725

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.