Hydrolysis of neutral glycerides by lipases of rat brain microsomes

Myles C. Cabot; Shimon Gatt

doi:10.1016/0005-2760(76)90264-2

Hydrolysis of neutral glycerides by lipases of rat brain microsomes

Myles C. Cabot
, Shimon Gatt

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

The hydrolysis of monoacylglycerol and diacylglycerol by rat brain microsomes was followed by measuring the release of glycerol and monooleylglycerol from dispersions of water insoluble glyceryl esters of oleic acid. The microsomes showed three lipolytic activities. One activity, optimal at pH 4.8, catalyzed the hydrolysis of diacylglycerol but not monoacylglycerol. Two other lipolytic activities, optimal at pH 8.0-8.6, catalyzed the hydrolysis of both diacylglycerol and monoacylglycerol. The pH 8.0-8.6 activities were sensitive to heat and SH-reagents. Detergents were inhibitory in all cases. Extraction of the microsomes with KCl, KSCN, urea or Triton X-100 did not change the ratio of diacylglycerol hydrolysis at pH 4.8 and 8.0. The results of subcellular fractionation studies showed that there was no significant enrichment of the acid lipase in any fraction.

Original language	English
Pages (from-to)	105-115
Number of pages	11
Journal	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume	431
Issue number	1
DOIs	https://doi.org/10.1016/0005-2760(76)90264-2
State	Published - 22 Apr 1976
Externally published	Yes

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title = "Hydrolysis of neutral glycerides by lipases of rat brain microsomes",

abstract = "The hydrolysis of monoacylglycerol and diacylglycerol by rat brain microsomes was followed by measuring the release of glycerol and monooleylglycerol from dispersions of water insoluble glyceryl esters of oleic acid. The microsomes showed three lipolytic activities. One activity, optimal at pH 4.8, catalyzed the hydrolysis of diacylglycerol but not monoacylglycerol. Two other lipolytic activities, optimal at pH 8.0-8.6, catalyzed the hydrolysis of both diacylglycerol and monoacylglycerol. The pH 8.0-8.6 activities were sensitive to heat and SH-reagents. Detergents were inhibitory in all cases. Extraction of the microsomes with KCl, KSCN, urea or Triton X-100 did not change the ratio of diacylglycerol hydrolysis at pH 4.8 and 8.0. The results of subcellular fractionation studies showed that there was no significant enrichment of the acid lipase in any fraction.",

author = "Cabot, \{Myles C.\} and Shimon Gatt",

note = "Funding Information: * Supported in part by NIH grant NS0296{\textquoteright}7. ** This work is part of a Ph.D. thesis to be submitted lem.",

year = "1976",

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doi = "10.1016/0005-2760(76)90264-2",

language = "English",

volume = "431",

pages = "105--115",

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T1 - Hydrolysis of neutral glycerides by lipases of rat brain microsomes

AU - Cabot, Myles C.

AU - Gatt, Shimon

N1 - Funding Information: * Supported in part by NIH grant NS0296’7. ** This work is part of a Ph.D. thesis to be submitted lem.

PY - 1976/4/22

Y1 - 1976/4/22

N2 - The hydrolysis of monoacylglycerol and diacylglycerol by rat brain microsomes was followed by measuring the release of glycerol and monooleylglycerol from dispersions of water insoluble glyceryl esters of oleic acid. The microsomes showed three lipolytic activities. One activity, optimal at pH 4.8, catalyzed the hydrolysis of diacylglycerol but not monoacylglycerol. Two other lipolytic activities, optimal at pH 8.0-8.6, catalyzed the hydrolysis of both diacylglycerol and monoacylglycerol. The pH 8.0-8.6 activities were sensitive to heat and SH-reagents. Detergents were inhibitory in all cases. Extraction of the microsomes with KCl, KSCN, urea or Triton X-100 did not change the ratio of diacylglycerol hydrolysis at pH 4.8 and 8.0. The results of subcellular fractionation studies showed that there was no significant enrichment of the acid lipase in any fraction.

AB - The hydrolysis of monoacylglycerol and diacylglycerol by rat brain microsomes was followed by measuring the release of glycerol and monooleylglycerol from dispersions of water insoluble glyceryl esters of oleic acid. The microsomes showed three lipolytic activities. One activity, optimal at pH 4.8, catalyzed the hydrolysis of diacylglycerol but not monoacylglycerol. Two other lipolytic activities, optimal at pH 8.0-8.6, catalyzed the hydrolysis of both diacylglycerol and monoacylglycerol. The pH 8.0-8.6 activities were sensitive to heat and SH-reagents. Detergents were inhibitory in all cases. Extraction of the microsomes with KCl, KSCN, urea or Triton X-100 did not change the ratio of diacylglycerol hydrolysis at pH 4.8 and 8.0. The results of subcellular fractionation studies showed that there was no significant enrichment of the acid lipase in any fraction.

UR - https://www.scopus.com/pages/publications/0017226682

U2 - 10.1016/0005-2760(76)90264-2

DO - 10.1016/0005-2760(76)90264-2

M3 - Article

C2 - 5151

AN - SCOPUS:0017226682

SN - 0005-2760

VL - 431

SP - 105

EP - 115

JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

IS - 1

ER -

Hydrolysis of neutral glycerides by lipases of rat brain microsomes

Abstract

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