Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels

Søren U. Nielsen; Anders O. Pedersen; Henrik Vorum; Rolf Brodersen

doi:10.1007/BF00231375

Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels

Søren U. Nielsen^*, Anders O. Pedersen, Henrik Vorum, Rolf Brodersen

^*Kontaktforfatter

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

6 Citationer (Scopus)

Abstract

A group of low molecular weight fatty acid-binding cytosolic proteins, FABP_c with high abundance in heart, liver, skeletal muscle, intestine and adipose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABP_c with M_T 15 kDa has been purified from human heart muscle and found to be present in levels 2-4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel electrophoresis under native and denaturing conditions has been used to characterize FABP_c from human heart and this protein is found to be a major protein of human heart myocytes. The pI of FABP_c from human heart was found to be about 5.3 under native conditions and about 6.5 in the presence of 9 M urea.

Originalsprog	Engelsk
Tidsskrift	Molecular and Cellular Biochemistry
Vol/bind	98
Udgave nummer	1-2
Sider (fra-til)	119-125
Antal sider	7
ISSN	0300-8177
DOI	https://doi.org/10.1007/BF00231375
Status	Udgivet - okt. 1990
Udgivet eksternt	Ja

Adgang til dokumentet

10.1007/BF00231375

AUB Link

Søg efter materialet i Aalborg Universitetsbiblioteks søgemaskine

Citationsformater

@article{52d2fd73f2114076a060f48a21e0a050,

title = "Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels",

abstract = "A group of low molecular weight fatty acid-binding cytosolic proteins, FABPc with high abundance in heart, liver, skeletal muscle, intestine and adipose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABPc with MT 15 kDa has been purified from human heart muscle and found to be present in levels 2-4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel electrophoresis under native and denaturing conditions has been used to characterize FABPc from human heart and this protein is found to be a major protein of human heart myocytes. The pI of FABPc from human heart was found to be about 5.3 under native conditions and about 6.5 in the presence of 9 M urea.",

keywords = "fatty acid-binding protein, human heart, native 2-D gel",

author = "Nielsen, {S{\o}ren U.} and Pedersen, {Anders O.} and Henrik Vorum and Rolf Brodersen",

year = "1990",

month = oct,

doi = "10.1007/BF00231375",

language = "English",

volume = "98",

pages = "119--125",

journal = "Molecular and Cellular Biochemistry",

issn = "0300-8177",

publisher = "Springer",

number = "1-2",

}

TY - JOUR

T1 - Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels

AU - Nielsen, Søren U.

AU - Pedersen, Anders O.

AU - Vorum, Henrik

AU - Brodersen, Rolf

PY - 1990/10

Y1 - 1990/10

N2 - A group of low molecular weight fatty acid-binding cytosolic proteins, FABPc with high abundance in heart, liver, skeletal muscle, intestine and adipose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABPc with MT 15 kDa has been purified from human heart muscle and found to be present in levels 2-4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel electrophoresis under native and denaturing conditions has been used to characterize FABPc from human heart and this protein is found to be a major protein of human heart myocytes. The pI of FABPc from human heart was found to be about 5.3 under native conditions and about 6.5 in the presence of 9 M urea.

AB - A group of low molecular weight fatty acid-binding cytosolic proteins, FABPc with high abundance in heart, liver, skeletal muscle, intestine and adipose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABPc with MT 15 kDa has been purified from human heart muscle and found to be present in levels 2-4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel electrophoresis under native and denaturing conditions has been used to characterize FABPc from human heart and this protein is found to be a major protein of human heart myocytes. The pI of FABPc from human heart was found to be about 5.3 under native conditions and about 6.5 in the presence of 9 M urea.

KW - fatty acid-binding protein

KW - human heart

KW - native 2-D gel

U2 - 10.1007/BF00231375

DO - 10.1007/BF00231375

M3 - Journal article

C2 - 2266953

AN - SCOPUS:0025074234

SN - 0300-8177

VL - 98

SP - 119

EP - 125

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

IS - 1-2

ER -

Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels

Abstract

Adgang til dokumentet

AUB Link

Fingeraftryk

Citationsformater