PMID- 1132395
OWN - NLM
STAT- MEDLINE
DCOM- 19750818
LR  - 20190918
IS  - 0013-9432 (Print)
IS  - 0013-9432 (Linking)
VI  - 19
IP  - 3
DP  - 1975
TI  - Glycolytic enzymes in the normal human term placenta.
PG  - 154-64
AB  - The enzymes hexokinase (HK), phosphoglucomutase (PGM), pyruvate kinase (PK) and 
      lactate dehydrogenase (LDH) were assayed in villous tissue homogenates and cell 
      fractions of normal human term placentas. Although lowest in activity and 
      probably rate limiting in glycolysis, hexokinase is theoretically adequate to 
      phosphorylate the total amount of glucose metabolized. PGM and PK activity were 
      in the same range exceeding HK by 10-15 times, suggesting a largely increased 
      breakdown of glycogen-derived glucose in situations of need. Substantially higher 
      LDH activities may reflect the placental ability to utilize lactate from both 
      mother and fetus. Of all enzymes only hexokinase was found to be associated with 
      the particulate matter in considerable amounts.
FAU - Gustke, H H
AU  - Gustke HH
FAU - Kowalewski, S
AU  - Kowalewski S
LA  - eng
PT  - Journal Article
PL  - Switzerland
TA  - Enzyme
JT  - Enzyme
JID - 1262265
RN  - EC 1.1.1.27 (L-Lactate Dehydrogenase)
RN  - EC 2.7.1.1 (Hexokinase)
RN  - EC 2.7.1.40 (Pyruvate Kinase)
RN  - EC 5.4.2.2 (Phosphoglucomutase)
SB  - IM
MH  - Female
MH  - *Glycolysis
MH  - Hexokinase/metabolism
MH  - Humans
MH  - L-Lactate Dehydrogenase/metabolism
MH  - Phosphoglucomutase/metabolism
MH  - Placenta/*enzymology
MH  - Pregnancy
MH  - Pyruvate Kinase/metabolism
MH  - Time Factors
EDAT- 1975/01/01 00:00
MHDA- 1975/01/01 00:01
CRDT- 1975/01/01 00:00
PHST- 1975/01/01 00:00 [pubmed]
PHST- 1975/01/01 00:01 [medline]
PHST- 1975/01/01 00:00 [entrez]
AID - 10.1159/000458987 [doi]
PST - ppublish
SO  - Enzyme. 1975;19(3):154-64. doi: 10.1159/000458987.