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  • Cell & Developmental Biology  (2)
  • Purification  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237 (1997)
    Springer
    Extremophiles 1 (1997), S. 151-156 
    Details
    ISSN: 1433-4909
    Keywords: Key wordsBacillus ; Alkaliphilic ; Alkaline ; Thermo-stable ; Cellulase ; Purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thermostable alkaline cellulase (endo-1,4-β-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-terminal amino acid sequence of the purified enzyme was Glu-Gly-Asn-Thr-Arg-Glu-Asp-Asn-Phe-Lys-His-Leu-Leu-Gly-Asn-Asp-Asn-Val-Lys-Arg. The enzyme had a molecular mass of approximately 86 kDa and an isoelectric point of pH 3.8. The enzyme had a pH optimum of 8.6–9.0 and displayed maximum activity at 45°C. The alkaline enzyme was stable up to 50°C and more than 30% of the original activity was detectable after heating at 100°C and at pH 9.0 for 10 min. The enzyme hydrolyzed carboxymethylcellulose, lichenan (β-1,3;1,4-linkage), and p-nitrophenyl derivatives of cellotriose and cellotetraose. Crystalline forms of cellulose (Avicel and filter paper), H3PO4-swollen cellulose, NaOH-swollen cellulose, curdlan (β-1,3-linkage), laminarin (β-1,3;1,6-linkage), and xylan were barely hydrolyzed at all.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050028
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and properties of mangano-superoxide dismutase from a strain of alkaliphilic Bacillus (1997)
    Springer
    Extremophiles 1 (1997), S. 74-78 
    Details
    ISSN: 1433-4909
    Keywords: Key words Superoxide dismutase ; Purification ; Alkaliphile ; Bacillus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A mangano-superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a strain of alkaliphilic Bacillus for the first time. The purified protein, with an isoelectric point of pH 4.5, had a molecular mass of approximately 50 kDa and consisted of two identical subunits (25 kDa). The N-terminal amino acid sequence was Ala-Tyr-Lys-Leu-Pro-Glu-Leu-Pro-Tyr-Ala-Ala-Asn-Ala-Leu-Glu-Pro-His-Ile-Asp-Glu-Ala. The optimum pH and temperature for the reaction were 7.5 and 35°C, respectively. The properties of the superoxide dismutase were compared with those of the enzyme from thermophilic Bacillus stearothermophilus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050017
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  • 3
    Electronic Resource
    Electronic Resource
    Transmission electron microscopy of critical point dried tissue after observation in the scanning electron microscopeThis work was supported by Ford Foundation grant 710-0036, NIDR grant T01-DE00278, and NIH grant AM 7578. (1973)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 176 (1973), S. 245-252 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Embryonic and adult rodent tissues were fixed and prepared for scanning electron microscopy by dehydration in ethanol followed by critical point drying with liquid carbon dioxide or Freon 13 (E. I. du Pont de Nemours, Inc.). After coating the dried specimens with evaporated metal, the tissues were studied by scanning microscopy. The same tissues were subsequently embedded in Epon-Araldite, thin sectioned and examined by transmission electron microscopy. The cytological details in these specimens were comparable to tissues embedded directly, without drying or metal-coating. With this technique it is possible to identify with greater certainty the structures responsible for surface contours revealed by the scanning electron microscope.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091760210
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  • 4
    Electronic Resource
    Electronic Resource
    The fine structure of bat spermatozoaResearch supported by grant RG 6729 from the National Institute of Health, United States Public Health Service. (1965)
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 116 (1965), S. 567-609 
    Details
    ISSN: 0002-9106
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The fine structure of epididymal spermatozoa of Myotis lucifugus and Eptesicus fuscus is described. Caudal to the acrosomal cap in both species, a thin intermediate layer is described as uniting the plasmalemma to the outer leaf of the nuclear envelope. Although this layer does not form a separate cap-like structure, it evidently corresponds to the “post nuclear cap” of light microscopists. A redundant portion of the nuclear envelope turns away from the condensed chromatin and continues caudad into the neck region where it forms a pair of concentric membrane systems on either side of the connecting piece. Two flattened mitochondria are closely applied to the dorsal and ventral aspects of the connecting piece.The sperm tails in the two species are generally similar except for the shape and distribution of mitochondria in the middle-piece and the thickness of the fibrous sheath of the principal piece. A unique arrangement of the mitochondria in Myotis makes it possible to determine the orientation of the plane of the central pair of flagellar fibrils in relation to the transverse axis of the flattened head and hence to deduce the probable plane of bending movments of the tail. Cortical and medullary zones are distinguished in the outer dense fibers of the flagellum and fibers 9, 1, 5, and 6 are consistently larger than the others. A set of slender satellite fibers are closely related to the inner aspect of the nine large outer fibers. Additional structural details of the axial filament complex are described, especially the cross-sectional configuration of the subfibrils in the doublets and their mode of termination in the end-piece. No “secondary fibers” or “mid fiber” were found.Since the axial filament complex of mammalian sperm tails is not continuous with a basal body, as in other flagella, it is suggested that the connecting piece is a centriolar derivative and may be the functional equivalent of a basal body for both the axial complex and the outer dense fibers.Comparisons are made of bat sperm tails and those of other mammalian species and the ultrastructure and arrangements of tail components are discussed in relation to the current concepts of sperm locomotion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001160306
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    Paper (German National Licenses)
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