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Relevant bibliographies by topics / Histidine dipeptides

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Academic literature on the topic 'Histidine dipeptides'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Histidine dipeptides"

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van Milgen, Jaap, and Nathalie Le Floc’h. "8 Functional Role of Histidine in Diets of Young Pigs." Journal of Animal Science 99, Supplement_1 (2021): 13. http://dx.doi.org/10.1093/jas/skab054.022.

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Abstract Histidine is a constituent amino acid of body proteins and, once incorporated in protein, histidine can be methylated post-translationally to methyl-histidine. Histidine is also a precursor of histamine, a neurotransmitter and involved in the immune response. Histidine and histamine are constituents of a number of dipeptides, which act as pH buffers, metal chelating agents, and anti-oxidants, especially in skeletal muscles and in the brain. A considerable fraction of whole-body histidine is present as carnosine, the dipeptide of histidine and β-alanine. In the longissimus muscle, abou

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Wang, Furong, Hailiang Shen, Ting Liu, Xi Yang, Yali Yang, and Yurong Guo. "Formation of Pyrazines in Maillard Model Systems: Effects of Structures of Lysine-Containing Dipeptides/Tripeptides." Foods 10, no. 2 (2021): 273. http://dx.doi.org/10.3390/foods10020273.

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At present, most investigations involving the Maillard reaction models have focused on free amino acids (FAAs), whereas the effects of peptides on volatile products are poorly understood. In our study, the formation mechanism of pyrazines, which were detected as characteristic volatiles in sunflower seed oil, from the reaction system of glucose and lysine-containing dipeptides and tripeptides was studied. The effect of the amino acid sequences of the dipeptides and tripeptides on pyrazine formation was further highlighted. Four different dipeptides and six tripeptides were selected. The result

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Heidenreich, Elena, Tilman Pfeffer, Tamara Kracke, et al. "A Novel UPLC-MS/MS Method Identifies Organ-Specific Dipeptide Profiles." International Journal of Molecular Sciences 22, no. 18 (2021): 9979. http://dx.doi.org/10.3390/ijms22189979.

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Background: Amino acids have a central role in cell metabolism, and intracellular changes contribute to the pathogenesis of various diseases, while the role and specific organ distribution of dipeptides is largely unknown. Method: We established a sensitive, rapid and reliable UPLC-MS/MS method for quantification of 36 dipeptides. Dipeptide patterns were analyzed in brown and white adipose tissues, brain, eye, heart, kidney, liver, lung, muscle, sciatic nerve, pancreas, spleen and thymus, serum and urine of C57BL/6N wildtype mice and related to the corresponding amino acid profiles. Results: A

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Skopicki, H. A., K. Fisher, D. Zikos, et al. "Carrier-mediated transport of pyroglutamyl-histidine in renal brush border membrane vesicles." American Journal of Physiology-Cell Physiology 255, no. 6 (1988): C822—C827. http://dx.doi.org/10.1152/ajpcell.1988.255.6.c822.

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These studies were performed to determine if a transmembrane carrier for pyroglutamyl-histidine (pGlu-His) is present in the luminal membrane of renal proximal tubular cells. Previous studies have suggested the intact transepithelial transport of pGlu-His, a dipeptide formed by the hydrolysis of luteinizing hormone-releasing hormone by enzymes associated with the brush border in the proximal nephron. With the use of a renal brush border membrane vesicle preparation, pGlu-His showed H+-stimulated, Na-independent, saturable transport into an osmotically active space. High-pressure liquid chromat

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Skopicki, H. A., K. Fisher, D. Zikos, G. Flouret, and D. R. Peterson. "Low-affinity transport of pyroglutamyl-histidine in renal brush-border membrane vesicles." American Journal of Physiology-Cell Physiology 257, no. 5 (1989): C971—C975. http://dx.doi.org/10.1152/ajpcell.1989.257.5.c971.

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These studies were performed to determine if a low-affinity carrier is present in the luminal membrane of proximal tubular cells for the transport of the dipeptide, pyroglutamyl-histidine (pGlu-His). We have previously described the existence of a specific, high-affinity, low-capacity [transport constant (Kt) = 9.3 X 10(-8) M, Vmax = 6.1 X 10(-12) mol.mg-1.min-1] carrier for pGlu-His in renal brush-border membrane vesicles. In the present study, we sought to demonstrate that multiple carriers exist for the transport of a single dipeptide by determining whether a low-affinity carrier also exist

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Ferranco, Annaleizle, Shibaji Basak, Alan Lough, and Heinz-Bernhard Kraatz. "Metal coordination of ferrocene–histidine conjugates." Dalton Transactions 46, no. 14 (2017): 4844–59. http://dx.doi.org/10.1039/c7dt00456g.

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Baldwin, J. "Identification of histidine dipeptides in monotreme muscle." Biochemical Systematics and Ecology 23, no. 7-8 (1995): 869–70. http://dx.doi.org/10.1016/0305-1978(95)00073-9.

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Song, Byeng Chun, Nam-Seok Joo, Giancarlo Aldini, and Kyung-Jin Yeum. "Biological functions of histidine-dipeptides and metabolic syndrome." Nutrition Research and Practice 8, no. 1 (2014): 3. http://dx.doi.org/10.4162/nrp.2014.8.1.3.

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Barbaresi, Silvia, Luc Maertens, Erik Claeys, Wim Derave, and Stefaan De Smet. "Differences in muscle histidine‐containing dipeptides in broilers." Journal of the Science of Food and Agriculture 99, no. 13 (2019): 5680–86. http://dx.doi.org/10.1002/jsfa.9829.

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Zhu, Xiao-fei, Min Fan, Xu-bin Wang, et al. "Hydrolysis of DNA by a Dipeptides Containing Histidine." International Journal of Peptide Research and Therapeutics 16, no. 4 (2010): 297–300. http://dx.doi.org/10.1007/s10989-010-9232-x.

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Dissertations / Theses on the topic "Histidine dipeptides"

1

White, Colleen A. "An investigation into human serum carnosinase." Thesis, Glasgow Caledonian University, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301471.

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Peterson, Maria Louise. "Effect of Feed Additives on Amino Acid and Dipeptide Transport by Intestines of American Lobster and Atlantic White Shrimp." UNF Digital Commons, 2014. http://digitalcommons.unf.edu/etd/497.

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Previous nutritional physiology research using L-histidine and zinc in American lobster intestine (Homarus americanus) has suggested that these solutes can be co-transported as complexes (Histidine-Zinc-Histidine) across the intestine using a peptide transporter. Furthermore, transport of L-leucine was shown to be inhibited by high calcium concentrations. Dipeptide and bis-complex transport and the role of calcium were investigated in the perfused intestines of lobster and Atlantic white shrimp (Litopenaeus setiferus). Following trans-intestinal transport, serosal medium was analyzed for amino

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Livisay, Stacy Ann. "Effect of oxidative stress on histidine containing dipeptides, conjugated linoleic acid and alpha-tocopherol in animal and human muscle." 1999. https://scholarworks.umass.edu/dissertations/AAI9950183.

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Skeletal muscle contains a number of endogenous antioxidants that aid in protecting the muscle from oxidative damage. Antioxidant systems are comprised of water and lipid soluble compounds. The histidine containing dipeptides, anserine and carnosine, and α-tocopherol represent water and lipid soluble antioxidants which protect the muscle from oxidative damage. Raw and cooked turkey thigh and breast muscle were oxidatively challenged in order to understand the role of water and lipid soluble antioxidants in protecting the muscle from oxidative damage. The data suggest both water soluble and lip

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Tessier, Christian. "Synthèse et caractérisation de complexes de technétium(V) et de rhénium(V) contenant des acides aminés et des dipeptides." Thèse, 2004. http://hdl.handle.net/1866/14345.

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McPhail, Olga Albert. "Analytical capillary electrophoresis of oxalate, histidine-containing dipeptides, melatonin and tryptophan metabolites, and taxol in the presence of cephalomannine and baccatin III." 1997. https://scholarworks.umass.edu/dissertations/AAI9737563.

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The high efficiency of capillary electrophoresis (CE) coupled with universality of direct UV absorbance detection allowed the quantification of the following matrices: (1) oxalate in numerous biological systems such as: human albumin, urine, parental nutrition solutions (intralipid infusion, multi-vitamin infusion), fifteen premature baby formulas produced by the two leading baby food companies, commercial skim and 1% fat milk emulsions; (2) histidine-containing antioxidants, carnosine and anserine, in pork and chicken muscle tissue extracts; (3) melatonin in the presence of the products of tr

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Books on the topic "Histidine dipeptides"

1

Skulachev, V., and V. P. Skulachev. Biological Significance of Histidine Containing Dipeptide (Soviet Scientific Reviews Series, Section D). Routledge, 1995.

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Book chapters on the topic "Histidine dipeptides"

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Aristoy, M. C., L. Mora, and F. Toldrá. "Histidine-containing Dipeptides: Properties and Occurrence in Foods." In Encyclopedia of Food and Health. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-384947-2.00777-7.

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Abe, Hiroki. "Chapter 14 Histidine-related dipeptides: distribution, metabolism, and physiological function." In Metabolic biochemistry. Elsevier, 1995. http://dx.doi.org/10.1016/s1873-0140(06)80017-2.

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Chow, C., V. Tatum, C. Yeh, et al. "Antioxidant Function of Carnosine, a Natural Histidine-Containing Dipeptide." In Proceedings of the International Symposium on Natural Antioxidants. AOCS Publishing, 1996. http://dx.doi.org/10.1201/9781439832059.ch16.

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4

"9. The potential evolution prototype of modern enzyme: Discovery of seryl–histidine dipeptide and its function." In Phosphorus Chemistry. De Gruyter, 2018. http://dx.doi.org/10.1515/9783110562552-009.

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