PMID- 3087977
OWN - NLM
STAT- MEDLINE
DCOM- 19860728
LR  - 20210210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 261
IP  - 18
DP  - 1986 Jun 25
TI  - Identification of a high affinity leukotriene C4-binding protein in rat liver 
      cytosol as glutathione S-transferase.
PG  - 8540-6
AB  - A soluble high affinity binding unit for leukotriene (LT) C4 in the high speed 
      supernatant of rat liver homogenate was characterized at 4 degrees C as having a 
      single type of saturable affinity site with a dissociation constant of 0.77 +/- 
      0.27 nM (mean +/- S.E., n = 5). The binding activity was identified as the liver 
      cytosolic subunit 1 (Ya) of glutathione S-transferase, commonly known as 
      ligandin, by co-purification with the catalytic activity during DEAE-cellulose 
      column chromatography and 11,12,14,15-tetrahydro-LTC4 (LTC2)-affinity gel column 
      chromatography; resolution into two major bands by sodium dodecyl 
      sulfate-polyacrylamide gel electrophoresis of Mr 23,000 and 25,000, of which only 
      the smaller protein was labeled with [3H]LTC4 coupled via a photoaffinity 
      cross-linking reagent; and immunodiffusion analysis with rabbit antiserum to 
      glutathione S-transferase which showed a line of identity between the purified 
      LTC4-binding protein and rat liver glutathione S-transferase. The 
      affinity-purified binding protein bound 800 pmol of [3H] LTC4/mg of protein and 
      possessed 12 mumol/min/mg of glutathione transferase activity as assayed with 
      1-chloro-2,4-dinitrobenzene as substrate. The enzyme activity of the cytosolic 
      LTC4-binding protein was inhibited by submicromolar quantities of unlabeled LTC4, 
      and the binding activity for [3H]LTC4 was blocked by the ligandin substrates, 
      hematin and bilirubin. The high affinity interaction between LTC4 and glutathione 
      S-transferase suggests that glutathione S-transferase may have a role in LTC4 
      disposition and that previous studies of LTC4 binding to putative receptors in 
      nonresponsive tissues may require redefinition of the binding unit.
FAU - Sun, F F
AU  - Sun FF
FAU - Chau, L Y
AU  - Chau LY
FAU - Spur, B
AU  - Spur B
FAU - Corey, E J
AU  - Corey EJ
FAU - Lewis, R A
AU  - Lewis RA
FAU - Austen, K F
AU  - Austen KF
LA  - eng
GR  - AI-22531/AI/NIAID NIH HHS/United States
GR  - AI-22563/AI/NIAID NIH HHS/United States
GR  - AI-23401/AI/NIAID NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Affinity Labels)
RN  - 0 (SRS-A)
RN  - EC 2.5.1.18 (Glutathione Transferase)
SB  - IM
MH  - Affinity Labels/metabolism
MH  - Animals
MH  - Cytosol/enzymology
MH  - Glutathione Transferase/*analysis
MH  - Immunodiffusion
MH  - Kinetics
MH  - Liver/*enzymology
MH  - Male
MH  - Mathematics
MH  - Molecular Weight
MH  - Photochemistry
MH  - Rats
MH  - SRS-A/*metabolism
MH  - Substrate Specificity
MH  - Tissue Distribution
EDAT- 1986/06/25 00:00
MHDA- 1986/06/25 00:01
CRDT- 1986/06/25 00:00
PHST- 1986/06/25 00:00 [pubmed]
PHST- 1986/06/25 00:01 [medline]
PHST- 1986/06/25 00:00 [entrez]
AID - S0021-9258(19)83944-3 [pii]
PST - ppublish
SO  - J Biol Chem. 1986 Jun 25;261(18):8540-6.