Abstract:
:Adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] was solubilized from a rat brain homogenate with sodium deoxycholate. This solubilized preparation had no detectable enzymic activity with either Mg-ATP or Mn-ATP as substrate. The activity could be restored by addition of either nonionic detergent or certain specific phospholipids. Maximal restoration of enzyme activity was obtained with Triton X-100, L-alpha-phosphatidylcholine, L-alpha-lysophosphatidylcholine, phosphatidyl-N-monomethylethanolamine, or sphingomyelin. Activity was only partially restored by phosphatidylethanolamine (40-60%) or phosphatidyl-N,N-dimethylethanolamine (10-20%). Other phospholipids tested, including phosphatidylserine, phosphatidylglycerol, phosphatidylinositol, and phosphatidic acid, could not restore enzyme activity but, instead, could inhibit the stimulation of enzyme activity by phosphatidylcholine. The restoration of activity by L-alpha-phosphatidylcholine was inhibited by cholesterol at concentrations above 33 mol %, although this effect was not observed with three different esters of cholesterol. These studies suggest a possible specific role of phospholipids in modulating adenylate cyclase activity.
journal_name
Proc Natl Acad Sci U S Aauthors
Hebdon GM,LeVine H 3rd,Sahyoun NE,Schmitges CJ,Cuatrecasas Pdoi
10.1073/pnas.78.1.120subject
Has Abstractpub_date
1981-01-01 00:00:00pages
120-3issue
1eissn
0027-8424issn
1091-6490journal_volume
78pub_type
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pub_type: 杂志文章,随机对照试验
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更新日期:2016-03-08 00:00:00
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更新日期:2015-04-14 00:00:00