2 edition of Purification and characterization of acylglycerol acyltransferases from rat intestine. found in the catalog.
Purification and characterization of acylglycerol acyltransferases from rat intestine.
Written in English
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|Number of Pages||255|
Beckman J. K., Coniglio J. G. () A comparative study of the lipid composition of isolated rat Sertoli and germinal cells. Lip – Crossref Medline, Google Scholar; 6. Grogan W. M., Lam J. W. () Fatty acid synthesis in isolated spermatocytes and spermatids of mouse testis. Lip – Crossref Medline, Google Cited by:
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Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells. Manganaro F, Kuksis A. We have purified the monoacylglycerol acyltransferase from rat small intestinal mucosa to homogeneity by a combination of hydrophobic absorption, guanidine dissociation, and gel by: Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells F.
Manganaro and, A. Kuksis Published on the web 26 April Cited by: important for fat absorption in human small intestine ().
Another acyltransferase, acyl-CoA independent MAG acyltransferase, has been purified to homogeneity from rat intestinal mucosa (17) whereas, acyl-CoA dependent MAG acyltransferase has not been purified from any source.
All the acyltransferases in these pathways are membrane. Kuksis A, Manganaro F. Biochemical characterization and purification of intestinal acylglycerol acyltransferases. In: Kuksis A, editor. Fat Absorption. CRC Press; Boca Raton: pp. – Lehner R, Kuksis A.
Triacylglycerol synthesis by purified triacylglycerol synthetase of rat intestinal mucosa. Role of acyl-CoA acyltransferase. Lehner, R.; Kuksis, A.; Itabashi, Y: Stereospecificity of monoacylglycerol and diacylglycerol acyltransferases from rat intestine as determined by chiral phase high-performance liquid chromatography.
Lipids, 28, 29–34 () PubMed CrossRef Google Scholar. Abstract. 1-Acyl-sn-glycerolphosphate acyltransferase (designated as PlsC in bacteria) catalyzes the acylation of lysophosphatidic acid and is responsible for the de novo production of phosphatidic acid, a precursor for the synthesis of various membrane e PlsC is an integral membrane protein, it is generally difficult to solubilize it without causing its Cited by: 4.
Protein acyltransferases (PATs) transfer a palmitoyl moiety derived from palmitoyl-CoA to a free thiol of a substrate protein to create a labile thioester linkage. Biochemical characterization and kinetic analysis of this new family of enzymes requires methods to purify PATs and their substrates, as well as methods to assay PAT by: Purification of PAT from rat livers.
Our purification protocol was considerably different than previous methods and took advantage of new knowledge and reagents for protein palmitoylation. We started with a plasma membrane fraction from rat livers because PAT activity toward G proteins is enriched in the plasma membrane fraction.
The Cited by: Phospholipid remodeling involves phospholipase activity to remove acyl chains and acyltransferases to replace acyl chains.
We here describe the characterization of a lysophospholipid acyltransferase in the opportunistic fungal pathogen, Candida sion of this gene, C.a. LPT1, complemented the lysophospholipid acyltransferase defect in Saccharomyces cerevisiae strains lacking the Cited by: 4.
THE JOURNAL OF BIOLOGICAL CHEMISTRY 0 by The American Society for Biochemistry and Molecular Biology, he. Val. 33, Issue of Novem pp.Printed in U.S.A.
Purification of an Acyl-CoA Hydrolase from Rat Intestinal Microsomes A CANDIDATE ACYL-ENZYME INTERMEDIATE IN GLYCEROLIPJD ACYLATION*Cited by: Abstract. During intestinal fat absorption, luminal lipolytic products are absorbed across the microvillus border of the enterocyte.
Inside the cell, lipolytic products are reesterified and assembled with apolipoproteins to yield chylomicrons, which are released at the basolateral membrane and enter the blood stream via the lymph (Black, ; Davidson, ).Cited by: 4.
Polyclonal antibodies against purified microsomal AAT from rat intestinal mucosa or IgGs from preimmune serum were bound to protein A agarose beads, the beads were washed twice with 10 column volumes of M sodium borate (pH ), and the IgGs were cross-linked to the protein A using 20 mM dimethylpimelimidate in 10 volumes of M sodium.
6Phosphogluconate Dehydrogenase: Purification, Characterization and Kinetic Properties from Rat Erythrocytes Article in Turkish Journal of Veterinary and Animal Sciences 28(4) January. THE JOURNAL OF BIOLOGICAL CHEMISTRY 8 by The American Society of Biological Chemists, Inc.
Vol.No. 1, Issue of January 5, pp.Printed in U. S.A. Monoacylglycerol Acyltransferase EVIDENCE THAT THE ACTIVITIES FROM RAT INTESTINE. METHODS IN ENZYMOLOGY, VOL. MONO- AND DIACYLGLYCEROL ACYLTRANSFERASES  99 Preparation of Microsomes from Rat Liver or Intestinal Mucosa Rat liver is minced with a pair of scissors and then homogenized in 9 volumes of STE buffer ( M sucrose, 10 mM Tris-HC1, pHmM EDTA) with a Teflon-glass homogenizer by 10 up-and-down Cited by: Partial Purification and Properties of Glycerophosphate Acyltransferase from Rat Liver.
Formation of 1-Acylglycerol 3-Phosphate from sn-Glycerol 3-Phosphate and Palmityl Coenzyme A. Glycerolphosphate is successively acylated at the sn-1 and sn-2 positions, catalyzed by glycerolphosphate acyltransferase (GPAT) (EC ) and 1-acylglycerolphosphate acyltransferase (or lysophosphatidic acid acyltransferase [LPAAT] [EC ]), respectively, yielding PA (, ).
Glycerolipid acyltransferases (including GPAT Cited by: The stereospecificity of monoacylglycerol acyltransferase from rat intestinal mucosa and suckling rat liver microsomes was examined using sn-1,2-diacylglycerol kinase from Escherichia coli. Purification and characterization. Biochim Biophys Acta.
Mar 7; (3)– Waite M, van Deenen LL. Hydrolysis of phospholipids and glycerides by rat-liver preparations. Biochim Biophys Acta. Jun 6; (3)– Waite M, Sisson P. Solubilization by heparin of the phospholipase A1 from the plasma membranes of rat by: human small intestine (14–16).
Another acyltransferase, acyl-CoA-independent MAG acyltransferase, has been purified to homogeneity from rat intestinal mucosa (17), whereas acyl-CoA-dependent MAG acyltransferase has not been purified from any source. All the acyltransferases in these pathways areCited by: Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells.
Can. Biochem. Cell Biol. Triacylglycerol synthesis by an sn-1,2(2,3)-diacylglycerol transacylase from rat intestinal microsomes Article (PDF Available) in Journal of Biological Chemistry (12) May with Purchase Phospholipid Biosynthesis, Volume - 1st Edition.
Print Book & E-Book. ISBNBook Edition: 1. Polokoff M. and Bell R. () Limited palmitoyl-CoA penetration into microsomal vesicles as evidenced by a highly latent ethanol acyltransferase activity. biol. Chem.Polokoff M. and Bell R. () Solubilization, partial purification and characterization of rat liver microsomal diacylglycerol by: 1.
Purification and characterization of d-glyceraldehydephosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus. European Journal of Biochemistry(1), DOI: /jtbx.
Hansjörg Eibl, Paul by: Previous studies by Coleman and Haynes (, J. Biol. Chem.) indicated the presence of two different tissue specific monoacylglycerol acyltransferases (MGAT) in intestinal mucosa and.
In enzymology, a 1-acylglycerolphosphate O-acyltransferase (EC ) is an enzyme that catalyzes the chemical reaction. acyl-CoA + 1-acyl-sn-glycerol 3-phosphate ⇌ CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Thus, the two substrates of this enzyme are acyl-CoA and 1-acyl-sn-glycerol 3-phosphate, whereas its two products are CoA and 1,2-diacyl-sn-glycerol : BRENDA entry.
The MBOAT enzyme family, identified incomprises 11 genes in the human genome that participate in a variety of biological processes. MBOAT enzymes contain multiple transmembrane domains and share two active site residues, histidine and asparagine. Several MBOAT members are drug targets for major human diseases, including atherosclerosis, obesity, Alzheimer disease, and viral Cited by: Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells.
Journal Can J Biochem Cell Biol (). Glicerolfosfat O-aciltransferaza (ECalfa-glicerofosfatna aciltransferaza, 3-glicerofosfatna aciltransferaza, ACP:sn-glicerolfosfatna aciltransferaza, glicerol 3-fosfatna aciltransferaza, glicerol fosfatna aciltransferaza, glicerol fosfatna transacilaza, glicerofosfatna aciltransferaza, glicerofosfatna transacilaza, sn-glicerol 3-fosfatna aciltransferaza, sn-glicerolfosfatna BRENDA: BRENDA entry.
The IUPHAR/BPS Guide to Pharmacology. monoacylglycerol O-acyltransferase 2 - Acyltransferases. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
Acyltransferases; Acyltransferases. Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn). GtoImmuPdb View OFF Expand all sections Collapse all sections.
Enzymes. Rat sn-glycerolphosphate acyltransferase: molecular cloning and characterization of the cDNA and expressed protein. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids(3), DOI: /S(99)Cited by: In enzymology, a 2-acylglycerol O-acyltransferase (EC ) is an enzyme that catalyzes the chemical reaction.
acyl-CoA + 2-acylglycerol ⇌ CoA + diacylglycerol. Thus, the two substrates of this enzyme are acyl-CoA and 2-acylglycerol, whereas its two products are CoA and diacylglycerol. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring BRENDA: BRENDA entry.
Sterol O-acyltransferase (also called Acyl-CoA cholesterol acyltransferase, Acyl-CoA cholesterin acyltransferase  or simply ACAT) is an intracellular protein located in the endoplasmic reticulum that forms cholesteryl esters from cholesterol.
Sterol O-acyltransferase catalyzes the chemical reaction. acyl-CoA + cholesterol ⇌ CoA + cholesterol esterBRENDA: BRENDA entry. Thus, the maintenance of a healthy physiological state is critically dependent on normal adipose tissue development and function.
The 1-acylglycerolphosphate-O-acyltransferases (AGPATs) catalyze the second step in the Kennedy pathway, acylating lysophosphatidic acid (LPA) with a fatty acyl-CoA at the sn-2 position, forming phosphatidic acid Author: Emily Mardian.
The partial purification (6-fold) and properties of a position and substrate specific acyl coenzyme A: sn-glycerolP acyltransferase from rat liver mitochondria are described. The preparation is devoid of acyl-CoA:monoacylglycerolP acyltransferase and lipid phosphomonoesterase activity.
AllFile Size: 1MB. The purpose of this review is to update the reader on our current understanding of the uptake and secretion of dietary lipid by the enterocyte to the periphery.
This is a multi-stage process that first involves luminal digestion, followed by cellular uptake and processing, and subsequent extracellular transport of chylomicrons. We discuss the importance of acid and pancreatic lipase in lipid Cited by: Gaustad R, Sletten K, Lovhaug D, Fonnum F (b) Purification and characterization of carboxylesterases from rat lung.
Biochem J – PubMed Google Scholar Gleason LN, Vough BP () Deformylation of 4,4-diformamidodiphenyl sulfone (DFD) by plasma of certain by: The monoacylglycerol pathway that occurs in the intestine during fat absorption will not be discussed.
Figure 1. Phosphatidic acid biosynthetic pathways. Mammalian Acyltransferases in Phosphatidic Acid Biosynthesis. GPAT activity has been known to be present in. This volume provides up-to-date information on the purification and characterization of the enzymes involved in phospholipid biosynthesis and on the mechanisms utilized by cells for the transfer of phospholipids.
It also includes protocols for generating phospholipid biosynthetic : $Monoacylglycerol lipase, also known as MAG lipase, acylglycerol lipase, MAGL, MGL or MGLL is an enzyme that, in humans, is encoded by the MGLL gene. MAGL is a kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases.
The catalytic triad has been identified as Ser, His, and BRENDA: BRENDA entry.Coleman, R.A.: Diacylglycerol acyltransferase and monoacylglycerol acyltransferase from liver and intestine. Methods Enzymol.,98– () PubMed CrossRef Google Scholar .