Rabbit phosphoglucose isomerase/neuroleukin/autocrine motility factor: Cloning via interspecies identity

Xiaochun Li, John Chirgwin

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Phosphoglucose isomerase is the first committed enzyme of glycolysis. The protein also has a variety of biological activities on mammalian cells. The molecular basis of these extracellular functions is unclear, and the high resolution three-dimensional structure of a mammalian enzyme has not been described. We report here the cDNA and protein sequence for phosphoglucose isomerase from rabbit muscle. The sequence was obtained directly by PCR without the need to screen clones from a cDNA library and encoded active enzyme when expressed in bacterial cells. The 558 amino acid rabbit coding sequence is the same length as and highly similar (92% residue identity) to the sequences from human and pig and less so (88%) to the mouse enzyme. Non- conservative amino acid changes between the four mammalian sequences are concentrated in the first 35 and last five residues. The rabbit protein has an additional Cys residue and amino acid changes at five positions otherwise invariant in the mammalian enzymes. (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)363-367
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1476
Issue number2
DOIs
StatePublished - Feb 9 2000
Externally publishedYes

Fingerprint

Glucose-6-Phosphate Isomerase
Cloning
Organism Cloning
Rabbits
Enzymes
Amino Acids
Proteins
Glycolysis
Bioactivity
Gene Library
Muscle
Swine
Complementary DNA
Clone Cells
Cells
Muscles
Polymerase Chain Reaction

Keywords

  • Autocrine motility factor
  • Neuroleukin
  • Phosphoglucose isomerase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

@article{64d73e85cd3b4a6988fb9f332bf1085e,
title = "Rabbit phosphoglucose isomerase/neuroleukin/autocrine motility factor: Cloning via interspecies identity",
abstract = "Phosphoglucose isomerase is the first committed enzyme of glycolysis. The protein also has a variety of biological activities on mammalian cells. The molecular basis of these extracellular functions is unclear, and the high resolution three-dimensional structure of a mammalian enzyme has not been described. We report here the cDNA and protein sequence for phosphoglucose isomerase from rabbit muscle. The sequence was obtained directly by PCR without the need to screen clones from a cDNA library and encoded active enzyme when expressed in bacterial cells. The 558 amino acid rabbit coding sequence is the same length as and highly similar (92{\%} residue identity) to the sequences from human and pig and less so (88{\%}) to the mouse enzyme. Non- conservative amino acid changes between the four mammalian sequences are concentrated in the first 35 and last five residues. The rabbit protein has an additional Cys residue and amino acid changes at five positions otherwise invariant in the mammalian enzymes. (C) 2000 Elsevier Science B.V.",
keywords = "Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase",
author = "Xiaochun Li and John Chirgwin",
year = "2000",
month = "2",
day = "9",
doi = "10.1016/S0167-4838(99)00258-7",
language = "English (US)",
volume = "1476",
pages = "363--367",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Rabbit phosphoglucose isomerase/neuroleukin/autocrine motility factor

T2 - Cloning via interspecies identity

AU - Li, Xiaochun

AU - Chirgwin, John

PY - 2000/2/9

Y1 - 2000/2/9

N2 - Phosphoglucose isomerase is the first committed enzyme of glycolysis. The protein also has a variety of biological activities on mammalian cells. The molecular basis of these extracellular functions is unclear, and the high resolution three-dimensional structure of a mammalian enzyme has not been described. We report here the cDNA and protein sequence for phosphoglucose isomerase from rabbit muscle. The sequence was obtained directly by PCR without the need to screen clones from a cDNA library and encoded active enzyme when expressed in bacterial cells. The 558 amino acid rabbit coding sequence is the same length as and highly similar (92% residue identity) to the sequences from human and pig and less so (88%) to the mouse enzyme. Non- conservative amino acid changes between the four mammalian sequences are concentrated in the first 35 and last five residues. The rabbit protein has an additional Cys residue and amino acid changes at five positions otherwise invariant in the mammalian enzymes. (C) 2000 Elsevier Science B.V.

AB - Phosphoglucose isomerase is the first committed enzyme of glycolysis. The protein also has a variety of biological activities on mammalian cells. The molecular basis of these extracellular functions is unclear, and the high resolution three-dimensional structure of a mammalian enzyme has not been described. We report here the cDNA and protein sequence for phosphoglucose isomerase from rabbit muscle. The sequence was obtained directly by PCR without the need to screen clones from a cDNA library and encoded active enzyme when expressed in bacterial cells. The 558 amino acid rabbit coding sequence is the same length as and highly similar (92% residue identity) to the sequences from human and pig and less so (88%) to the mouse enzyme. Non- conservative amino acid changes between the four mammalian sequences are concentrated in the first 35 and last five residues. The rabbit protein has an additional Cys residue and amino acid changes at five positions otherwise invariant in the mammalian enzymes. (C) 2000 Elsevier Science B.V.

KW - Autocrine motility factor

KW - Neuroleukin

KW - Phosphoglucose isomerase

UR - http://www.scopus.com/inward/record.url?scp=0033982038&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033982038&partnerID=8YFLogxK

U2 - 10.1016/S0167-4838(99)00258-7

DO - 10.1016/S0167-4838(99)00258-7

M3 - Article

C2 - 10669800

AN - SCOPUS:0033982038

VL - 1476

SP - 363

EP - 367

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -