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Results: 411 to 415 of 415

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Physical properties of collagen--sodium dodecyl sulfate complexes.
Freytag JW, Noelken ME, Hudson BG
(1979) Biochemistry 18: 4761-8
MeSH Terms: Animals, Cattle, Circular Dichroism, Collagen, Kinetics, Molecular Weight, Protein Binding, Protein Conformation, Proteins, Skin, Sodium Dodecyl Sulfate
Show Abstract · Added December 10, 2013
Sodium dodecyl sulfate (NaDodSO4)--polyacrylamide gel electrophoresis and gel filtration chromatography of protein--NaDodSO4 complexes are frequently used to characterize collagen-like polypeptide components in mixtures obtained from extracts of basement membranes. However, electrophoresis yields anomalously high apparent molecular weights for collagenous polypeptides when typical globular proteins are used as molecular weight standards, and the use of gel filtration chromatography for this purpose was suspect because Nozaki et al. [Nozaki, Y., Schechter, N. M., Reynolds, J. A., & Tanford, C. (1976) Biochemistry 15, 3884--3890] found that asymmetric particles, including NaDodSO4--protein complexes, coeluted with native globular proteins of lower Stokes radius, when Sepharose 4B was used. To understand these effects and to improve the characterization of collagenous polypeptides, we investigated the secondary structure of NaDodSO4--collagen complexes with the use of circular dichroism, measured the NaDodSO4 content, studied the dependence of electrophoretic mobility on gel concentration, and extended work on gel filtration by use of a more porous gel, Sepharose CL-4B. We found that the anomalous behavior of collagen chains on NaDodSO4--polyacrylamide gel electrophoresis is due in large part to treatment of data and that the method can be used to determine rather accurate values for the number of residues per polypeptide chain. Our gel filtration results indicated that reliable molecular weights can be obtained when Sepharose CL-4B is used. These methods can be applied equally well to collagenous and noncollagenous polypeptides.
1 Communities
1 Members
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11 MeSH Terms
Primary hemostasis (collagen-platelet interaction): introduction.
Cunningham LW, Santoro S, Davies H
(1978) Suppl Thromb Haemost 63: 205-13
MeSH Terms: Animals, Blood Platelets, Calcium, Collagen, Hemostasis, Humans, Platelet Aggregation, Rats, Skin Physiological Phenomena, Wound Healing
Added March 5, 2014
1 Communities
1 Members
0 Resources
10 MeSH Terms
Glucagonoma syndrome in a 19-year-old woman.
Riddle MC, Golper TA, Fletcher WS, Ensinck JW, Smith PH
(1978) West J Med 129: 68-72
MeSH Terms: Adenoma, Islet Cell, Adult, Female, Glucagon, Humans, Neoplasm Metastasis, Pancreatic Neoplasms, Skin Manifestations, Syndrome
Added August 10, 2015
0 Communities
1 Members
0 Resources
9 MeSH Terms
Collagen-mediated platelet aggregation. Evidence for multivalent interactions of intermediate specificity between collagen and platelets.
Santoro SA, Cunningham LW
(1977) J Clin Invest 60: 1054-60
MeSH Terms: Amino Acids, Animals, Borohydrides, Carbohydrates, Chemical Phenomena, Chemistry, Collagen, Hot Temperature, Humans, In Vitro Techniques, Oxidation-Reduction, Periodic Acid, Platelet Aggregation, Protein Denaturation, Rats, Skin, Sodium Chloride, Solubility
Show Abstract · Added March 5, 2014
We have shown previously that periodate oxidation of collagen carbohydrate does not affect its ability to aggregate platelets. We now describe an additional characterization of periodate-modified collagen which demonstrates that collagen devoid of intact carbohydrate is fully capable of fibril formation, and we confirm its capacity to initiate platelet aggregation. Furthermore, we demonstrate that the platelet aggregating abilities of Types I, II, and III fibrillar collagen are quite similar despite differences in carbohydrate content and amino acid sequence. We also demonstrate that monomeric, pepsin-solubilized Type I human collagen is ineffective inhibiting aggregation by performed fibrils derived from the same molecule, thus establishing that the affinity of platelets for collagen depends upon prior polymerization of collagen. We interpret these and other findings to demonstrate that the hydroxylysyl glycoside regions of collagen are not highly specific sites involved in platelet-collagen interactions leading to "physiological" aggregation, and that the possibility must be considered that multiple interactions involving collagen sites of comparatively low structural specificity may be the initiating events in release of platelet ADP and the ensuing aggregation.
1 Communities
1 Members
0 Resources
18 MeSH Terms
Comparative studies on highly metabolically active histone acetylation.
Moore M, Jackson V, Sealy L, Chalkley R
(1979) Biochim Biophys Acta 561: 248-60
MeSH Terms: Acetylation, Animals, Cell Cycle, Cell Division, Cell Line, Dactinomycin, Histone Deacetylases, Histones, Liver Neoplasms, Experimental, Mitosis, Neoplasm Proteins, Skin, Tetrahymena pyriformis, Thymus Gland
Show Abstract · Added March 5, 2014
Histone acetate is hydrolyzed rapidly in logarithmically dividing hepatoma tissue culture cells (Jackson, V., Shires, A., Chalkley, R. and Granner, D.K. (1975) J. Biol. Chem. 250, 4856--4863). The phenomenon has been analyzed further in hepatoma tissue culture cells at various stages of the cell cycle, in stationary phase, and in the presence of actinomycin D. We also investigated the phenomenon in Tetrahymena pyriformis macronuclei, bovine thymocytes, and human foreskin fibroblasts. The data suggest that this highly metabolically active histone acetylation while altered in mitotic cells, is independent of the overall rate of cell division, and is only slightly sensitive to actinomycin D. Finally, we conclude that the same general phenomenon is found in both cancerous and normal cells and is apparently common to cells from various stages of the evolutionary scale.
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1 Members
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14 MeSH Terms