PMID- 3432124
OWN - NLM
STAT- MEDLINE
DCOM- 19880302
LR  - 20190818
IS  - 0196-9781 (Print)
IS  - 0196-9781 (Linking)
VI  - 8
IP  - 5
DP  - 1987 Sep-Oct
TI  - Inhibition of the reactivation of acid-dissociated lactate dehydrogenase 
      isoenzymes by their aminoterminal CNBr fragments.
PG  - 773-8
AB  - The catalytic activity of lactate dehydrogenase isoenzymes (LDH) depends on their 
      tetrameric structure. Stabilization of this quaternary structure is achieved by 
      interaction of the N-terminal part of one subunit with the C-terminal region of 
      the other subunit. The N-terminal peptides from pig M-LDH and H-LDH which are 
      responsible for this stabilization were obtained by CNBr-fragmentation and 
      purification on reversed-phase HPLC. The effect of these peptides on the 
      formation of the quaternary structure of LDH-isoenzymes was investigated by 
      monitoring the reconstitution of the catalytic activity after acid-dissociation. 
      Low concentrations of the N-terminal peptides led to an increased, and high 
      concentrations to a decreased yield of reconstituted LDH activity. The effects of 
      these two peptides were isoenzyme specific. The 32 residue peptide derived from 
      M-LDH showed the highest effect when tested with M-LDH as target enzyme but only 
      a poor effect with H-LDH. On the other side the 33 residue peptide generated from 
      H-LDH showed a moderate effect with both isoenzymes. The effects of the 
      N-terminal LDH peptides are antagonized by the coenzymes NAD+ and NADH. The most 
      significant influence was observed with NAD+ in the M-LDH peptide-M-LDH enzyme 
      system. Comparison of the properties of the reactivation antagonists isolated 
      from human origin with the N-terminal CNBr-peptides of LDH revealed identity in 
      all essential properties, suggesting that the former peptides are generated by 
      degradation of LDH.
FAU - Dobeli, H
AU  - Dobeli H
AD  - Research Department, Kantonsspital, Basel, Switzerland.
FAU - Gillessen, D
AU  - Gillessen D
FAU - Lergier, W
AU  - Lergier W
FAU - Van Dijk, A
AU  - Van Dijk A
FAU - Schoenenberger, G A
AU  - Schoenenberger GA
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Peptides
JT  - Peptides
JID - 8008690
RN  - 0 (Isoenzymes)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Peptide Fragments)
RN  - EC 1.1.1.27 (L-Lactate Dehydrogenase)
RN  - OS382OHJ8P (Cyanogen Bromide)
SB  - IM
MH  - Animals
MH  - Cyanogen Bromide
MH  - Enzyme Activation
MH  - Female
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Isoenzymes
MH  - Kinetics
MH  - L-Lactate Dehydrogenase/antagonists & inhibitors/*metabolism
MH  - Macromolecular Substances
MH  - Muscles/enzymology
MH  - Peptide Fragments/antagonists & inhibitors/*metabolism
MH  - Placenta/enzymology
MH  - Swine
EDAT- 1987/09/01 00:00
MHDA- 1987/09/01 00:01
CRDT- 1987/09/01 00:00
PHST- 1987/09/01 00:00 [pubmed]
PHST- 1987/09/01 00:01 [medline]
PHST- 1987/09/01 00:00 [entrez]
AID - 0196-9781(87)90057-X [pii]
AID - 10.1016/0196-9781(87)90057-x [doi]
PST - ppublish
SO  - Peptides. 1987 Sep-Oct;8(5):773-8. doi: 10.1016/0196-9781(87)90057-x.