دورية أكاديمية

Partial purification and properties of mammalian phosphatidylglycerophosphatase.

التفاصيل البيبلوغرافية
العنوان: Partial purification and properties of mammalian phosphatidylglycerophosphatase.
المؤلفون: MacDonald PM, McMurray WC
المصدر: Biochimica et biophysica acta [Biochim Biophys Acta] 1980 Oct 06; Vol. 620 (1), pp. 80-9.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam : Elsevier Pub. Co.
مواضيع طبية MeSH: Mitochondria, Liver/*enzymology , Phosphoric Monoester Hydrolases/*isolation & purification, Animals ; Cations, Divalent/pharmacology ; Chromatography, Gel ; Hydrogen-Ion Concentration ; Phosphoric Monoester Hydrolases/metabolism ; Rats
مستخلص: The phosphatidylglycerophosphatase (EC 3.1.3.27) activity of rat liver mitochondria was investigated by assaying the conversion of 14C-labelled phosphatidylglycerophosphate to phosphatidylglycerol. The activity was associated with a mitochondrial membrane fraction and could not be released into solution employing techniques applicable to a peripheral membrane protein. The enzyme was partially purified by sonication, pH 5.0 precipitation, and gel filtration. Various ionic and nonionic detergents as well as numerous divalent cations inhibited the phosphatase. The enzyme displayed a high affinity for phosphatidylglycerophosphate.
المشرفين على المادة: 0 (Cations, Divalent)
EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
EC 3.1.3.27 (phosphatidylglycerophosphatase)
تواريخ الأحداث: Date Created: 19801006 Date Completed: 19801216 Latest Revision: 20190609
رمز التحديث: 20240627
DOI: 10.1016/0005-2760(80)90187-3
PMID: 6251897
قاعدة البيانات: MEDLINE
الوصف
تدمد:0006-3002
DOI:10.1016/0005-2760(80)90187-3