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Figure 1 | BMC Structural Biology

Figure 1

From: Progesterone modulation of transmembrane helix-helix interactions between the α-subunit of Na/K-ATPase and phospholipid N-methyltransferase in the oocyte plasma membrane

Figure 1

Time course of [3H]Methyl incorporation into PME and SM. Upper: The steps involved in phosphatidylethanolamine (PE) N-methylation and sphingomyelin (SM) synthesis) in R. Pipiens oocyte plasma membranes involving PE, phosphatidylmonomethylethanolamine (PME), phosphatidyldimethylethanolamine (PDE), phosphatidylcholine (PC) and sphingomyelin (SM. Lower: Net increase in S-adenosyl methionine-derived 3H ([3H]SAM) incorporation into PME and SM in isolated plasma-vitelline membranes as a function of time after addition of progesterone. The values shown are calculated from 3H migrating with phospholipid standards using one-dimensional TLC and are expressed as fmols per 10 membranes corrected for basal levels of the individual phospholipids at the times points indicated. 1,2-DAG (1,2-diacylglycerol) is the product of SM synthase. Values are means ± SEM for oocytes from 3 females.

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BMC Structural Biology

ISSN: 1472-6807

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