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  • 1
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    Concentration, Mobility and Profit Rates (1969)
    Oxford : Periodicals Archive Online (PAO)
    Economic Inquiry. 7:3 (1969:Sept.) 276 
    Details
    ISSN: 0095-2583
    Topics: Economics
    Description / Table of Contents: INDUSTRIAL ORGANIZATION; TECHNOLOGICAL CHANGE; INDUSTRY STUDIES
    Notes: ABSTRACTS OF PAPERS, FORTY-FOURTH ANNUAL CONFERENCE, WESTERN ECONOMIC ASSOCIATION
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:b097-1969-007-03-000065
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  • 2
    Electronic Resource
    Electronic Resource
    Potassium-selective ion channels in a transformed insulin-secreting cell line (1987)
    Springer
    The journal of membrane biology 95 (1987), S. 63-72 
    Details
    ISSN: 1432-1424
    Keywords: K+ channel ; patch clamp ; single-channel recording ; HIT cells ; insulin secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary K+ channels in inside-out patches from hamster insulin tumor (HIT) cells were studied using the patch-clamp technique. HIT cells provide a convenient system for the study of ion channels and insulin secretion. They are easy to culture, form gigaohm seals readily and secrete insulin in response to glucose. The properties of the cells changed with the passage number. For cell passage numbers 48 to 56, five different K+-selective channels ranging from 15 to 211 pS in symmetrical 140mm KCl solutions were distinguished. The channels were characterized by the following features: a channel with a conductance (in symmetrical 140mm KCl solutions) of 210 pS that was activated by noncyclic purine nucleotides and closed by H+ ions (pH=6.8); a 211 pS channel that was Ca2+-activated and voltage dependent; a 185 pS channel that was blocked by TEA but was insensitive to quinine or nucleotides; a 130 pS channel that was activated by membrane hyperpolarization; and a small conductance (15 pS) channel that was not obviously affected by any manipulation. As determined by radioimmunoassay, cells from passage number 56 secreted 917±128 ng/mg cell protein/48 hr of insulin. In contrast, cells from passage number 77 revealed either no channel activity or an occasional nonselective channel, and secreted only 29.4±8.5 ng/mg cell protein/48 hr of insulin. The nonselective channel found in the passage 77 cells had a conductance of 25 pS in symmetrical 140mm KCl solutions. Thus, there appears to be a correlation between the presence of functional K+ channels and insulin secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869631
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  • 3
    Electronic Resource
    Electronic Resource
    Ultrastructural immunocytochemical localization of l-glutamate decarboxylase and GABA in rat pancreatic zymogen granules (1988)
    Springer
    Cell & tissue research 252 (1988), S. 191-197 
    Details
    ISSN: 1432-0878
    Keywords: GABA ; Glutamate decarboxylase ; GABA transaminase ; Exocrine pancreas ; Immunocytochemistry ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The ultrastructural immunohistochemical localization of gamma aminobutyric acid (GABA) and its regulating enzymes, l-glutamate decarboxylase (GAD) and gamma aminobutyrate-α-ketoglutarate transaminase, was determined utilizing an immunogold post-embedding protocol in pancreatic exocrine tissue. Within the acinar cell, GABA and its biosynthetic enzyme, GAD, were localized in zymogen granules. Quantitative analysis of the GABA immunoreactivity in the acinar cell revealed 1.7±0.5 gold particles/μm2 over the cytoplasm, 36.6±14.1 gold particles/ μm2 over the zymogen granules, and 2.9±2.1 gold particles /μm2 over the mitochondria. Quantitative analysis of the distribution of colloidal gold particles, representing glutamate decarboxylase immunoreactivity in the acinar cells, revealed 38.4±2.5 gold particles/μm2 over the zymogen granules, 4.7±1.1 gold particles/μm2 over the mitochondria and 6.3±0.5 gold particles/μm2 over the remainder of the cytoplasm. Substitution of normal sheep serum for the sheep anti-glutamate decarboxylase serum revealed a significant (p〈 0.001) decrease of the colloidal gold particle distribution over the zymogen granules and cytoplasmic compartments of the acini. Gamma aminobutyrate -α-ketoglutarate transaminase, the catabolic enzyme for GABA, was not detected in the mitochondria, zymogen granules, and cytoplasm of the acinar cell, suggesting that GABA is not catabolized within the acinar cell. Preabsorption and substitution controls resulted in an absence of labeling. These results suggest that GABA may act extracellularly and/or have a role within the zymogen granule in the exocrine pancreas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00213841
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