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  • 1985-1989  (4)
  • 1970-1974
  • 1965-1969  (4)
  • 1905-1909
  • 1890-1899
  • 1986  (4)
  • 1966  (4)
  • 1907
  • 1897
  • Proteins
  • 1
    ISSN: 1432-2242
    Keywords: Electrophoresis ; Endosperm ; Proteins ; Wild emmer ; Wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The relative proportion and amount of proteins in five defined molecular weight (MW) regions (A1=above 71,000=71K, A2=71K−49K, A3=49K−31K, A4=31K−20K, A5=20K and less) were estimated by densitometric analyses of the amount of dye bound by kernel proteins (Fullington et al. 1980) of Triticum dicoccoides SDS-PAGE gels. These MW regions roughly correspond to the wheat protein solubility classes (Cole et al. 1981; Fullington et al. 1983). One purpose of the study was to select accessions whose seed proteins bind relatively high amounts of dye in the glutenin and albumin globulin regions. These accessions will be used for further in-depth studies as possible candidate donors of genes to improve the baking and nutritional quality of wheat. Marked differences in the quantitative relationships were found among the proteins in the five MW regions. Coefficients of variation (CV's) for the highest peak (i.e., most abundant protein) MW in different protein MW regions were similar for A1, A2 and A3, at 11.4, 11.7, and 11.1%, respectively, but only 4.1 for A4, and 10.6% for region A5. The CV for the highest peak MW overall was 29.8. Accession BP0649, for example, had over 44% of its protein in region A5, whereas BP0566 (lowest among the top 10%) had only 21.4% of its protein in that region. Over 37% of the proteins of accessions BP0649 and 0001 to 0005 was in region A5. At least 84 accessions with the highest amount of protein in region A5, and 13 accessions with more protein in region A1 than Chinese Spring may merit further evaluation as possible protein gene donors. High amounts of protein in A1 may be of importance in bread-baking quality, and in A4 and A5 for high lysine wheat. Accessions in both extremes were selected to test these hypotheses. All accessions are now or will be available in the USDA Wheat Collection.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 73 (1986), S. 47-52 
    ISSN: 1432-2242
    Keywords: Cucurbita pepo L. ; Isoelectric focusing ; Proteins ; Single pollen grain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Isoelectric focusing of proteins from single pollen grains of Cucurbita pepo L. has been developed for large scale study of pollen grain populations' heterogeneity. Forty to forty-five protein bands from one pollen grain are revealed after silver staining. Applications of this technique to pollen grain populations from different genotypes are described in this paper. Possible applications and limits of this technique are discussed with respect to plant breeding especially for the measure of gene frequencies in pollen grain populations.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 22 (1986), S. 388-390 
    ISSN: 1612-1112
    Keywords: Size exclusion chromatography ; Proteins ; Optimization of resolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Optimization strategies for improvement of peak capacity in size exclusion chromatography (SEC) of proteins with chemically modified silica columns are discussed. Decreasing flow rate and particle diameter and increasing the pore volume per unit column volume help to improve peak capacity in SEC.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 25 (1986), S. 535-552 
    ISSN: 0570-0833
    Keywords: HPLC (high pressure liquid chromatography) ; Proteins ; Analytical methods ; Chromatography ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The application of high-pressure liquid chromatography (HPLC) to proteins has undergone a dramatic development in recent years. Nowadays its many variants expand the repertoire of high-performance analysis methods available to the protein chemist, which, until now, have been dominated by electrophoretic techniques. The advent of gene technology has resulted in a renaissance of protein chemistry. The new analytical and preparative problems that have thereby emerged are often ideally solved by HPLC methods. HPLC has long since ceased to be solely a laboratory technique; HPLC systems are now being developed for the separation of proteins-particularly those of great pharmaceutical interest - on a 100-g scale. The range of applications of analytical and preparative HPLC will be illustrated by two examples of pharmaceutical importance - insulin and interleukin 2.
    Additional Material: 23 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 231-245 
    ISSN: 0570-0833
    Keywords: Quaternary structure ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Many protein molecules, particularly those with high molecular weights, consist not of a single polypeptide chain, but form a complex made up from several polypeptide chains. This structure, which can be reversibly broken down, is known as the quaternary structure. A number of metabolic phenomena can be explained on a molecular basis by invoking the quaternary structure.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 558-566 
    ISSN: 0570-0833
    Keywords: Casein ; Milk ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Casein from cow's milk is not a single substance, but can be resolved into numerous components. These include x-casein, which is the only fraction that contains appreciable quantities of sugars. This component plays a very important role in the clotting of milk by rennin, when it is split into an almost sugar-free fraction, para-x-casein, and a fraction containing sugars, x-caseinoglycopeptide. Caseinoglycopeptides have been isolated not only from the casein of cow's milk, but also from the caseins of sheep. Goat, and human milk. The second part of the paper deals with the clotting of milk by rennin and the amino acid sequence in caseinoglycopeptides.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 798-806 
    ISSN: 0570-0833
    Keywords: Evolution ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The evolution of protein structures is discussed using cytochrome c, hemoglobin, and neurohypophyseal hormones as examples. Although these substances have different biological functions, their evolution is controlled by the same general rules: their primary structures vary at the level of the species, order, or class, but this variation is restricted by the fact that the biological activity of the protein must not be impaired. Alterations (i.e. substitutions, deletions, or additions of amino acid residues) can therefore occur only in certain positions of the peptide chains, although with different frequencies. The total number of alterations thus represents only the final state of a protein and does not take into account successive substitutions which may have taken place at the affected sites. It can therefore give only a rough indication of the phylogenetic distance between two species. The nature of the substituting residues, on the other hand, is a useful guide to zoological cognateness, since it allows the identification of transition molecules which simultaneously contain amino acid residues from the protein of the protein of the evolutionary ancestor and from the protein of the evolutionary descendant.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 807-822 
    ISSN: 0570-0833
    Keywords: Insulin ; Hormones ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The protein hormone insulin occurs widely in the animal kingdom. Although its biological function is always the same, its amino-acid composition varies widely. Insulin consists of two polypeptide chains, which are linked by three cystine residues to form a bicyclic system with a 20-membered and an 85-membered ring. The protein crystallizes in various forms with foreign ions. In solution, insulin normally forms aggregates of 2n molecules. The hormone can be regenerated from the separated polypeptide chains, and its total synthesis has been achieved in a similar manner from synthesized peptide chains. In the biosynthesis of insulin, the two chains are evidently built up separately and subsequently linked together. Insulin promotes the synthesis of glycogen, fat, and protein in the organism; insulin deficiency leads to an increase in the blood-sugar level. At the molecular level, the mechanism of action of the hormone is still unknown. Current hypotheses are discussed. No specific active center has so far been detected in the insulin molecule, which contains several antigenic regions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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