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  • Biochemistry and Biotechnology  (4)
  • Cell & Developmental Biology  (3)
  • 1
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The polypeptide patterns obtained from individual caryopses (kernels) of two wheat cultivars were analyzed using high resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) methods. While few polypeptides were detected with Coomassie Blue staining methods, over two hundred peptides were easily distinguished with the color-based silver stain. The relative isoelectric points of the constituent polypeptides ranged from pH 3.8 to 9 and the relative molecular weights from 5000 to 200 000. The majority of the proteins of the two wheat varieties analyzed with 2-D PAGE were similar although distinct proteins having molecular weights of 23 000, 30 000, 37 000 and 70 000 were identified, which have molecular properties unique to each variety. The use of the color-based silver stain makes it possible to identify and characterize hundreds of proteins in individual wheat seeds. These methods are, therefore, adaptable for the rapid analysis and characterization of specific gene products of single kernels of wheat.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A rapid laboratory method for processing quality color prints of high resolution two-dimensional polyacrylamide gels has been developed to obtain photographs for data storage or for the presentation of results in poster formats. This method involves the contact printing of a gel directly onto the film so that the final print will be an exact duplication of the size and color of the gel. A variety of papers or films can be used to produce color prints or transparencies. This method has been adapted for use with a color or with a black and white photographic enlarger.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 2 (1987), S. 330-339 
    ISSN: 0887-3585
    Keywords: van der Waals radii ; conformation ; amino acid residue ; dipeptide approximation ; molecular modeling ; systematic conformationl search ; N-alkyl amino acid ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Effective van der Waals radii were celebrated in such a way that molecular models built from standard bond lengths and bond angels reproduced the amino acid conformations observed by crystallography in proteins and peptides. The celebrations were based on the comparision of the Ramachandbran plots prepared from high-resolution X-ray data of protins and peptides with the allowed φ,ψ torsional angel space for the depeptide molecular models. The celebrated radii are useful as criteria with which to filter energetically improbable conformations in molecular modeling studies of proteins and peptides.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 25 (1990), S. 339-344 
    ISSN: 1040-452X
    Keywords: Fertilization ; Oocyte investments ; Cumulus matrix ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have examined the proteins associated with the mucous matrix of the rat cumulus oophorus and compared them to the composition of rat serum, follicular fluid, ampullary fluid, and oocyte-cumulus cell extract. The cumulus matrix was dispersed using Streptomyces hyaluronidase, and the proteins were analyzed by highresolution two-dimensional polyacrylamide gel electrophoresis and compared with proteins of the serum, proestrous follicular fluid, and postvulatory ampullary fluid and extracts of oocytes and cumulus cells. In addition to albumin and transferrin, which were common to all the fluids analyzed, the cumulus material contained many proteins in common with the follicular fluid and the ampullary fluid. However, the protein extract of the cumulus matrix also contained four major proteins not present in the other fluids analyzed. Two of these proteins were acidic and heterogenous in charge and size (MW ∼81,000 and 100,000). The other two proteins were more basic and occurred at MW ∼90,000 and 150,000. Our results show that the extracellular matrix of the cumulus contains proteins that are not present in the fluids that surround the oocyte.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 309-319 
    ISSN: 0730-2312
    Keywords: guinea pig ; kallikrein ; nerve growth-factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Guinea pig prostate contains one major soluble esteropeptidase activity. The protein has been purified and characterized and found to be a glycoprotein comprised of a single polypeptide chain. The molecular weight of the deglycosylated protein is approximately 26,000. The esteropeptidase has a similar Km for lysine and arginine synthetic substrates, although the Vmax for arginine is much greater than that for lysine. Amino-terminal sequence analysis has also revealed a marked degree of homology to mouse γ-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to γ-NGF, however, the guinea pig enzyme does not appear to form stable complexes with β-NGF.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 33 (1987), S. 65-75 
    ISSN: 0730-2312
    Keywords: precursor ; hormone ; limited proteolysis ; submandibular gland ; prostate ; nerve growth factor ; epidermal growth factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Hormones and growth factors are generally released from larger precursors by limited proteolysis. The causative agents remain poorly defined with respect to location and properties. One subset of proteases, the glandular kallikreins, have been implicated in a few cases, in part because of their specific association with mature forms of some hormones. However, limited distribution and low copy number in some species cast doubt on this hypothesis, and they may well play other physiological functions that remain to be elucidated.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 54-57 
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A rapid, inexpensive method for the salt-free concentration of small quantities of proteins for analysis by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) has been developed. Proteins adsorbed to diatomaceous earth are subsequently removed using either sodium dodecyl sulfate or urea solubilization reagents for 2D-PAGE analysis. This procedure has been found to concentrate proteins having wide ranges of molecular weight and charge. It is also valuable for the concentration of large numbers of small samples from cells cultured in vitro.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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