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  • hemoglobin  (2)
  • Cell lysis  (1)
  • Enamel  (1)
  • Springer  (4)
  • 1975-1979  (4)
Collection
Publisher
  • Springer  (4)
Years
  • 1975-1979  (4)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 26 (1978), S. 139-142 
    ISSN: 1432-0827
    Keywords: Chemisorption ; Surface area ; Hydroxyapatite ; Bone ; Enamel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The surface areas of three different samples of hydroxyapatite, samples of deproteinized bone, and samples of whole and deproteinized enamel were determined by adsorption of an adduct (the diglycidyl ether of bisphenol A with N-phenylglycine) from methylene chloride solution. In all cases, the surface areas of these samples agree well with those obtained by the BET (N2) method.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4927
    Keywords: crustacean ; hemoglobin ; polyacrylamide electrophoresis ; Artemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two loci account for all genetic variation resulting in difference in electrophoretic mobility in three hemoglobins (Hb1, Hb2, and HbX) in the hemolymph of the brine shrimp. Four α alleles and nine β alleles have been studied. In shrimps of all genotypes and in electrophoresis in media with varying degrees of molecular sieving, Hb2 is approximately equidistant from Hb1 and HbX. A shrimp heterozygous at both loci has a three-banded Hb1, a four-banded Hb2, and a three-banded HbX. We conclude that Hb2 contains n α-polypeptides and n β-polypeptides. Hb1 contains 2n α-polypeptides. HbX contains 2n β-polypeptides. During electrophoresis, the three native hemoglobins undergo reversible dissociation to n subunits. Subunits with the same charge reassemble to migrate as molecules of the same size as the native molecules. Although there is no evidence for an additional polypeptide in the three hemoglobins, we cannot exclude such a possibility. If it exists, it is under three constraints: (1) it must be present in equal amounts in each of the three hemoglobins; (2) it must have the same molecular weight as the α- and β-polypeptides; and (3) it must be free of genetic variation (detectable by electrophoresis).
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 15 (1977), S. 423-437 
    ISSN: 1573-4927
    Keywords: hemoglobin ; polyacrylamide electrophoresis ; crustacean ; Artemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Electrophoretic mobilities of three hemoglobins (Hb1, Hb2, and Hb3) were studied in 15 populations of brine shrimps. Genetic segregation data support the model that Hb2 contains n α-polypeptides and n β-polypeptides; Hb1 contains 2n α-polypeptides. Hb3 contains neither α- nor β-polypeptides. There is no evidence of linkage of α and β loci with each other or with the locus (or loci) which governs Hb3 or with the nonhomologous portion of the sex chromosomes. Hemoglobins of different populations may be hybridized in vitro by incubation at high temperature. Reversible dissociation to subunits which contain only one (α or β) polypeptide occurs at 40 C (for Hb1) and at 50 C (for Hb2).
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0878
    Keywords: Pore cells ; Fine structure ; Acid phosphatase ; Cell lysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine structure of the pore cells in pre- and post-hatched Deroceras reticulatum is described. The cells have been divided into three main types on morphological grounds, one type being particularly rich in glycogen. Certain pore cells contain haemocyanin granules in grooves below cytoplasmic tongues, and in characteristic double-membrane-bounded vesicles within dilated cisternae of rough endoplasmic reticulum, as well as in other identified areas. All types of pore cells show fine fibres reminiscent of collagen associated with the basal lamina and pore complexes. In addition to acid phosphatase activity in lysosomes and Golgi elements, intra- and extracisternal activity has been demonstrated in association with the rough endoplasmic reticulum. The intracisternal activity is in close proximity to the Golgi apparatus and may represent enzyme that is about to enter the GERL system. Extracisternal activity may be associated with cellular lysis and death, or may represent local areas of degradation leading to cytodifferentiation. Remnants of lysed pore cells appear to be taken up by connective tissue amoebocytes.
    Type of Medium: Electronic Resource
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