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Identification of chemical oviposition stimulants from rice grain forSitophilus zeamais motschulsky (Coleoptera, Curculionidae).

Journal of chemical ecology

Maeshima K, Hayashi N, Murakami T, Takahashi F, Komae H.
PMID: 24311091
J Chem Ecol. 1985 Jan;11(1):1-9. doi: 10.1007/BF00987598.

Chemical components stimulating oviposition bySitophilus zeamais in rice grain were isolated from rice bran and were found to be a mixture of ferulates, diglycerides, and free sterols. Oviposition preference of the species can be induced by synergistic action of...

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Maeshima K, Hayashi N, Murakami T, et al. Identification of chemical oviposition stimulants from rice grain forSitophilus zeamais motschulsky (Coleoptera, Curculionidae). J Chem Ecol. 1985;11(1):1-9doi: 10.1007/BF00987598.
Maeshima, K., Hayashi, N., Murakami, T., Takahashi, F., & Komae, H. (1985). Identification of chemical oviposition stimulants from rice grain forSitophilus zeamais motschulsky (Coleoptera, Curculionidae). Journal of chemical ecology, 11(1), 1-9. https://doi.org/10.1007/BF00987598
Maeshima, K, et al. "Identification of chemical oviposition stimulants from rice grain forSitophilus zeamais motschulsky (Coleoptera, Curculionidae)." Journal of chemical ecology vol. 11,1 (1985): 1-9. doi: https://doi.org/10.1007/BF00987598
Maeshima K, Hayashi N, Murakami T, Takahashi F, Komae H. Identification of chemical oviposition stimulants from rice grain forSitophilus zeamais motschulsky (Coleoptera, Curculionidae). J Chem Ecol. 1985 Jan;11(1):1-9. doi: 10.1007/BF00987598. PMID: 24311091.
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Skeletal muscle-specific CPT1 deficiency elevates lipotoxic intermediates but preserves insulin sensitivity.

Journal of diabetes research

Shi W, Hu S, Wang W, Zhou X, Qiu W.
PMID: 24319696
J Diabetes Res. 2013;2013:163062. doi: 10.1155/2013/163062. Epub 2013 Nov 11.

OBJECTIVE: By specific knockout of carnitine palmitoyl transferase 1b (CPT1b) in skeletal muscles, we explored the effect of CPT1b deficiency on lipids and insulin sensitivity.METHODS: Mice with specific knockout of CPT1b in skeletal muscles (CPT1b M-/-) were used for...

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Shi W, Hu S, Wang W, et al. Skeletal muscle-specific CPT1 deficiency elevates lipotoxic intermediates but preserves insulin sensitivity. J Diabetes Res. 2013;2013:163062doi: 10.1155/2013/163062.
Shi, W., Hu, S., Wang, W., Zhou, X., & Qiu, W. (2013). Skeletal muscle-specific CPT1 deficiency elevates lipotoxic intermediates but preserves insulin sensitivity. Journal of diabetes research, 2013163062. https://doi.org/10.1155/2013/163062
Shi, Wanchun, et al. "Skeletal muscle-specific CPT1 deficiency elevates lipotoxic intermediates but preserves insulin sensitivity." Journal of diabetes research vol. 2013 (2013): 163062. doi: https://doi.org/10.1155/2013/163062
Shi W, Hu S, Wang W, Zhou X, Qiu W. Skeletal muscle-specific CPT1 deficiency elevates lipotoxic intermediates but preserves insulin sensitivity. J Diabetes Res. 2013;2013:163062. doi: 10.1155/2013/163062. Epub 2013 Nov 11. PMID: 24319696; PMCID: PMC3844227.
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Acyl migration solid phase isomerization of 1,2-diglycerides to 1,3-isomers.

Lipids

De Groot WT.
PMID: 27519572
Lipids. 1972 Sep;7(9):626-8. doi: 10.1007/BF02531967.

In mixtures of 1,2- and 1,3-diglycerides stored some degrees below their melting points, a rather rapid isomerization of almost all the 1,2- diglycerides to the 1,3-isomers occurred. This solid-phase isomerization leads to a substantial increase in the yield of...

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De Groot WT. Acyl migration solid phase isomerization of 1,2-diglycerides to 1,3-isomers. Lipids. 1972;7(9):626-8doi: 10.1007/BF02531967.
De Groot, W. T. (1972). Acyl migration solid phase isomerization of 1,2-diglycerides to 1,3-isomers. Lipids, 7(9), 626-8. https://doi.org/10.1007/BF02531967
De Groot, W T. "Acyl migration solid phase isomerization of 1,2-diglycerides to 1,3-isomers." Lipids vol. 7,9 (1972): 626-8. doi: https://doi.org/10.1007/BF02531967
De Groot WT. Acyl migration solid phase isomerization of 1,2-diglycerides to 1,3-isomers. Lipids. 1972 Sep;7(9):626-8. doi: 10.1007/BF02531967. PMID: 27519572.
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Anthophora Bees: Unusual Glycerides from Maternal Dufour's Glands Serve as Larval Food and Cell Lining.

Science (New York, N.Y.)

Norden B, Batra SW, Fales HM, Hefetz A, Shaw GJ.
PMID: 17759841
Science. 1980 Mar 07;207(4435):1095-7. doi: 10.1126/science.207.4435.1095.

The Dufour's gland of Anthophora abrupta, a solitary bee, secretes a complex mixture of liquid triglycerides containing one long-chain and two shortchain fatty acids. This is applied inside the earthen brood cells and added to the provision, where it...

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Norden B, Batra SW, Fales HM, et al. Anthophora Bees: Unusual Glycerides from Maternal Dufour's Glands Serve as Larval Food and Cell Lining. Science. 1980;207(4435):1095-7doi: 10.1126/science.207.4435.1095.
Norden, B., Batra, S. W., Fales, H. M., Hefetz, A., & Shaw, G. J. (1980). Anthophora Bees: Unusual Glycerides from Maternal Dufour's Glands Serve as Larval Food and Cell Lining. Science (New York, N.Y.), 207(4435), 1095-7. https://doi.org/10.1126/science.207.4435.1095
Norden, B, et al. "Anthophora Bees: Unusual Glycerides from Maternal Dufour's Glands Serve as Larval Food and Cell Lining." Science (New York, N.Y.) vol. 207,4435 (1980): 1095-7. doi: https://doi.org/10.1126/science.207.4435.1095
Norden B, Batra SW, Fales HM, Hefetz A, Shaw GJ. Anthophora Bees: Unusual Glycerides from Maternal Dufour's Glands Serve as Larval Food and Cell Lining. Science. 1980 Mar 07;207(4435):1095-7. doi: 10.1126/science.207.4435.1095. PMID: 17759841.
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Identification of an acyl donor in steryl ester biosynthesis by enzyme preparations from spinach leaves.

Plant physiology

Garcia RE, Mudd JB.
PMID: 16660515
Plant Physiol. 1978 Sep;62(3):348-53. doi: 10.1104/pp.62.3.348.

A pathway for steryl ester biosynthesis in acetone powder preparations from spinach (Spinacia oleracea L.) leaves has been elucidated; free sterol and 1,2-diglyceride were the substrates. Although animals synthesize cholesteryl esters by three distinct biosynthetic pathways, none of these...

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Garcia RE, Mudd JB. Identification of an acyl donor in steryl ester biosynthesis by enzyme preparations from spinach leaves. Plant Physiol. 1978;62(3):348-53doi: 10.1104/pp.62.3.348.
Garcia, R. E., & Mudd, J. B. (1978). Identification of an acyl donor in steryl ester biosynthesis by enzyme preparations from spinach leaves. Plant physiology, 62(3), 348-53. https://doi.org/10.1104/pp.62.3.348
Garcia, R E, and Mudd, J B. "Identification of an acyl donor in steryl ester biosynthesis by enzyme preparations from spinach leaves." Plant physiology vol. 62,3 (1978): 348-53. doi: https://doi.org/10.1104/pp.62.3.348
Garcia RE, Mudd JB. Identification of an acyl donor in steryl ester biosynthesis by enzyme preparations from spinach leaves. Plant Physiol. 1978 Sep;62(3):348-53. doi: 10.1104/pp.62.3.348. PMID: 16660515; PMCID: PMC1092124.
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Characterization of fatty acids from root and shoot lipids ofCapsicum species.

Lipids

Lyons JM, Lippert LF.
PMID: 17805668
Lipids. 1966 Mar;1(2):136-40. doi: 10.1007/BF02533006.

Lipids were extracted from the roots and shoots of four species of theCapsicum (pepper) genus and separated into three fractions: triglycerides; free fatty acids, mono- and diglycerides; and phospholipids. The component fatty acids were determined by subjecting the methyl...

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Lyons JM, Lippert LF. Characterization of fatty acids from root and shoot lipids ofCapsicum species. Lipids. 1966;1(2):136-40doi: 10.1007/BF02533006.
Lyons, J. M., & Lippert, L. F. (1966). Characterization of fatty acids from root and shoot lipids ofCapsicum species. Lipids, 1(2), 136-40. https://doi.org/10.1007/BF02533006
Lyons, J M, and Lippert, L F. "Characterization of fatty acids from root and shoot lipids ofCapsicum species." Lipids vol. 1,2 (1966): 136-40. doi: https://doi.org/10.1007/BF02533006
Lyons JM, Lippert LF. Characterization of fatty acids from root and shoot lipids ofCapsicum species. Lipids. 1966 Mar;1(2):136-40. doi: 10.1007/BF02533006. PMID: 17805668.
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Pancreatic lipase hydrolysis as a source of diglycerides for the stereospecific analysis of triglycerides.

Lipids

Anderson RE, Bottino NR, Reiser R.
PMID: 17805710
Lipids. 1967 Sep;2(5):440-2. doi: 10.1007/BF02531864.

No abstract available.

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Anderson RE, Bottino NR, Reiser R. Pancreatic lipase hydrolysis as a source of diglycerides for the stereospecific analysis of triglycerides. Lipids. 1967;2(5):440-2doi: 10.1007/BF02531864.
Anderson, R. E., Bottino, N. R., & Reiser, R. (1967). Pancreatic lipase hydrolysis as a source of diglycerides for the stereospecific analysis of triglycerides. Lipids, 2(5), 440-2. https://doi.org/10.1007/BF02531864
Anderson, R E, et al. "Pancreatic lipase hydrolysis as a source of diglycerides for the stereospecific analysis of triglycerides." Lipids vol. 2,5 (1967): 440-2. doi: https://doi.org/10.1007/BF02531864
Anderson RE, Bottino NR, Reiser R. Pancreatic lipase hydrolysis as a source of diglycerides for the stereospecific analysis of triglycerides. Lipids. 1967 Sep;2(5):440-2. doi: 10.1007/BF02531864. PMID: 17805710.
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A comparative study of the lipids of globule membrane and fat core and of the milk serum of cows.

Lipids

Huang TC, Kuksis A.
PMID: 17805787
Lipids. 1967 Nov;2(6):453-60. doi: 10.1007/BF02533171.

Nine samples of fresh raw cow's milk were separated into fat globules and milk serum by centrifugation. After destabilization by freezing and thawing, the milk fat globules were resolved into membranes and fat cores. The lipid composition of these...

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Huang TC, Kuksis A. A comparative study of the lipids of globule membrane and fat core and of the milk serum of cows. Lipids. 1967;2(6):453-60doi: 10.1007/BF02533171.
Huang, T. C., & Kuksis, A. (1967). A comparative study of the lipids of globule membrane and fat core and of the milk serum of cows. Lipids, 2(6), 453-60. https://doi.org/10.1007/BF02533171
Huang, T C, and Kuksis, A. "A comparative study of the lipids of globule membrane and fat core and of the milk serum of cows." Lipids vol. 2,6 (1967): 453-60. doi: https://doi.org/10.1007/BF02533171
Huang TC, Kuksis A. A comparative study of the lipids of globule membrane and fat core and of the milk serum of cows. Lipids. 1967 Nov;2(6):453-60. doi: 10.1007/BF02533171. PMID: 17805787.
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The incorporation of(14)C-glycerol into different species of diglycerides and triglycerides in rat liver slices.

Lipids

Hill EE, Lands WE, Slakey SP.
PMID: 17805819
Lipids. 1968 Sep;3(5):411-6. doi: 10.1007/BF02531279.

The relative rates of de novo synthesis of species of diglycerides and triglycerides from(14)C-glycerol were examined in rat liver slices. Diglycerides containing one or two double bonds per molecule and triglycerides containing four or more double bonds per molecule...

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Hill EE, Lands WE, Slakey SP. The incorporation of(14)C-glycerol into different species of diglycerides and triglycerides in rat liver slices. Lipids. 1968;3(5):411-6doi: 10.1007/BF02531279.
Hill, E. E., Lands, W. E., & Slakey, S. P. (1968). The incorporation of(14)C-glycerol into different species of diglycerides and triglycerides in rat liver slices. Lipids, 3(5), 411-6. https://doi.org/10.1007/BF02531279
Hill, E E, et al. "The incorporation of(14)C-glycerol into different species of diglycerides and triglycerides in rat liver slices." Lipids vol. 3,5 (1968): 411-6. doi: https://doi.org/10.1007/BF02531279
Hill EE, Lands WE, Slakey SP. The incorporation of(14)C-glycerol into different species of diglycerides and triglycerides in rat liver slices. Lipids. 1968 Sep;3(5):411-6. doi: 10.1007/BF02531279. PMID: 17805819.
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Digestion of butyrate glycerides by pancreatic lipase.

Lipids

Sampugna J, Quinn JG, Pitas RE, Carpenter DL, Jensen RG.
PMID: 17805699
Lipids. 1967 Sep;2(5):397-402. doi: 10.1007/BF02531853.

The racemic triglycerides, glyceryl-1-palmitate-2,3-dibutyrate (PBB), glyceryl-1-butyrate-2,3-dipalmitate (PPB), glyceryl-2-butyrate-1,3-dipalmitate (PBP), and the diglyceride, racemic glyceryl-1-palmitate-3-butyrate (P-B) were synthesized and digested with pancreatic lipase. Each triglyceride was mixed with equimolar amounts of triolein (OOO) prior to incubation.The following order of digestion...

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Sampugna J, Quinn JG, Pitas RE, et al. Digestion of butyrate glycerides by pancreatic lipase. Lipids. 1967;2(5):397-402doi: 10.1007/BF02531853.
Sampugna, J., Quinn, J. G., Pitas, R. E., Carpenter, D. L., & Jensen, R. G. (1967). Digestion of butyrate glycerides by pancreatic lipase. Lipids, 2(5), 397-402. https://doi.org/10.1007/BF02531853
Sampugna, J, et al. "Digestion of butyrate glycerides by pancreatic lipase." Lipids vol. 2,5 (1967): 397-402. doi: https://doi.org/10.1007/BF02531853
Sampugna J, Quinn JG, Pitas RE, Carpenter DL, Jensen RG. Digestion of butyrate glycerides by pancreatic lipase. Lipids. 1967 Sep;2(5):397-402. doi: 10.1007/BF02531853. PMID: 17805699.
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Determination of the structure of lecithins via the formation of acetylated 1,2-diglycerides.

Lipids

Privett OS, Nutter LJ.
PMID: 17805742
Lipids. 1967 Mar;2(2):149-54. doi: 10.1007/BF02530915.

A detailed procedure for quantitative determinations of molecular species of lecithins is described and applied to several lecithins isolated from natural sources. The method is based on the conversion of lecithin to acetylated 1,2-diglycerides and analysis of these compounds...

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Privett OS, Nutter LJ. Determination of the structure of lecithins via the formation of acetylated 1,2-diglycerides. Lipids. 1967;2(2):149-54doi: 10.1007/BF02530915.
Privett, O. S., & Nutter, L. J. (1967). Determination of the structure of lecithins via the formation of acetylated 1,2-diglycerides. Lipids, 2(2), 149-54. https://doi.org/10.1007/BF02530915
Privett, O S, and Nutter, L J. "Determination of the structure of lecithins via the formation of acetylated 1,2-diglycerides." Lipids vol. 2,2 (1967): 149-54. doi: https://doi.org/10.1007/BF02530915
Privett OS, Nutter LJ. Determination of the structure of lecithins via the formation of acetylated 1,2-diglycerides. Lipids. 1967 Mar;2(2):149-54. doi: 10.1007/BF02530915. PMID: 17805742.
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Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions.

Biotechnology and bioengineering

Stamatis H, Xenakis A, Dimitriadis E, Kolisis FN.
PMID: 18623049
Biotechnol Bioeng. 1995 Jan 05;45(1):33-41. doi: 10.1002/bit.260450106.

The activity of purified Pseudomonas cepacia lipase has been investigated in esterification reactions of various aliphatic alcohols with natural fatty acids. The reactions were carried out in microemulsions formed in isooctane by bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT). Kinetic studies showed...

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Stamatis H, Xenakis A, Dimitriadis E, et al. Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions. Biotechnol Bioeng. 1995;45(1):33-41doi: 10.1002/bit.260450106.
Stamatis, H., Xenakis, A., Dimitriadis, E., & Kolisis, F. N. (1995). Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions. Biotechnology and bioengineering, 45(1), 33-41. https://doi.org/10.1002/bit.260450106
Stamatis, H, et al. "Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions." Biotechnology and bioengineering vol. 45,1 (1995): 33-41. doi: https://doi.org/10.1002/bit.260450106
Stamatis H, Xenakis A, Dimitriadis E, Kolisis FN. Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions. Biotechnol Bioeng. 1995 Jan 05;45(1):33-41. doi: 10.1002/bit.260450106. PMID: 18623049.
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Showing 1 to 12 of 99 entries