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  • Chemical Engineering  (127)
  • General Chemistry  (63)
  • Cell & Developmental Biology  (60)
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  • 1
    Digitale Medien
    Digitale Medien
    Letters to the editor (1988)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 34 (1988), S. 1931-1936 
    Details
    ISSN: 0001-1541
    Schlagwort(e): Chemistry ; Chemical Engineering
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/aic.690341124
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Polymorphic assembly of subtilisin-cleaved tubulin (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 31-38 
    Details
    ISSN: 0886-1544
    Schlagwort(e): microtubule assembly ; proleolysis ; Vinca drugs ; Zn2+-induced assembly ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Limited proteolysis of tubulin with subtilisin results in cleavage of both the α and β subunits, releasing small peptides from the C-terminal ends. At 37°C the digested tubulin assembles into polymorphic structures: microtubules with attached ribbons in the presence of GTP, rings in the presence of GDP, and protofilament spirals in the presence of vinblastine. Undigested tubulin does not assemble under these conditions. Rings and Vinca-induced spiral structures are assembled from undigested tubulin only when microtubule-associated proteins, high Mg2+ concentrations, or polycations are present. Thus, cleavage with subtilisin affects assembly in a manner similar to the addition of these agents. It appears that binding of positively charged substances may act by neutralizing the charge on the highly acidic C-terminal regions of the α- and β-subunits, while cleavage with subtilisin produces the same effect by removing these peptides. Undigested and subtilisin-digested tubulin form sheets of protofilaments in the presence of Zn2+, which indicates that the binding sites for the 2-3 Zn2+ ions necessary to induce sheet formation do not reside in the C-terminal regions of the monomers.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970070105
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  • 3
    Digitale Medien
    Digitale Medien
    Structure and mass analysis of 12S and 19S dynein obtained from bull sperm flagella (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 368-374 
    Details
    ISSN: 0886-1544
    Schlagwort(e): STEM ; polypeptide composition ; ciliary motility ; dynein molecule ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: The Brookhaven scanning transmission electron microscpe (STEM) was used to elucidate the structures and masses of 12S and 19S dynein extracted from bull sperm flagella. The 12S particle was a single globular particle with an average mass of 311 ± 10 kdaltons. The 19S dynein particles consisted of two globular heads joined to a common base. The average mass of the 19S particle was 1.6 ± 0.04 × 106 daltons. Thus, with the exception of the larger mass, the bull sperm 19S dynein molecule resembles the two-headed 21S dynein obtained from sea urchin sperm flagella and the 18S dynein obtained from Chlamydomonas with the possibility of a third head giving rise to the 12S particle. The structure, mass and polypeptide composition of bull sperm flagella dynein is compared with outer arm dyneins previously obtained from Chlamydomonas, Tetrahymena, and sea urchin sperm flagella.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970080409
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  • 4
    Digitale Medien
    Digitale Medien
    LC20 and kinetics of gizzard myosin subfragment-1: Digestion with papain vs. S. aureus protease (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 23 (1992), S. 213-221 
    Details
    ISSN: 0886-1544
    Schlagwort(e): actin-activated ATPase ; LC20 cleavage ; phosphorylation ; HMM ; actin affinity ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Previous reports have shown that papain-digested gizzard subfragment-1 (PAP-S1) has a cleaved regulatory light chain (LC20), and Vmax similar to phosphorylated heavy meromyosin (HMM) Greene et al., Biochemistry 22:530-535, 1983; Sellers et al., J. Biol. Chem. 257:13880-13883, 1982; Umemoto et al., [J. Biol. Chem. 264:1431-1436, 1989], while S. aureus protease-digested S-1 (SAP-S1) has intact LC20, but Vmax closer to that of unphosphorylated HMM [Ikebe and Hartshorne, 1985]. To determine whether intact LC20 inhibits ATPase activity for subfragment- 1 (S1), we compared the kinetic properties and structures of unphosphorylated PAP-S1 and SAP-S1. SDS-PAGE showed that SAP-S1 had 68 and 24 KDa heavy chain and 20 and 17 KDa light chain components. PAP-S1 (15 minutes digestion at 20°C) also had 68 and 17 KDa bands, but the single 24 KDa band (24HC) was replaced by a group of 22-24 KDa fragments and LC20 was cleaved to a 16 KDa fragment. At 13 mM ionic strength, both PAP-S1 and SAP-S1 had Vmax similar to phosphorylated HMM (1.1-1.5 s-1). SAP-S1 had the same KATPase as phosphorylated HMM (38 μM actin). but KATPase for PAP-S1 was 3-fold stronger (11 μM actin). Subsequent digestion of SAP-S1 with papain did not significantly change Vmax, but as LC20 and 24HC were cleaved, both KATPase and Kbinding strengthened 3- to 5-fold. Thus, intact LC20 did not inhibit, and cleavage of LC20 did not increase Vmax for S1. Rather, papain cleavage of LC20 and 24HC was associated with strengthened actin binding. © 1992 Wiley-Liss, Inc.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970230305
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  • 5
    Digitale Medien
    Digitale Medien
    Smooth muscle myosin subfragment-1 is a kinetic analogue for heavy meromyosin in the extended conformation (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 26 (1993), S. 291-300 
    Details
    ISSN: 0886-1544
    Schlagwort(e): conformational transition ; single turnover assays ; ionic strength ; S1/S2 junction ; actin-activated ATPase activity ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: The 10S→6S (Flexed→Extended) transition in smooth muscle myosin is related to increased ATPase activity, but there is controversy over whether the analogous 9S→7S transition in HMM is also associated with ATPase activity. We therefore studied the association of ionic strength, phosphorylation, and ATPase activity for HMM as compared to S1 which has no apparent flexed conformation. In addition, we performed both steady state and single turnover analyses, to control for artifacts due to multiple subfragment populations that might skew steady state results.At low ionic strength where myosin and HMM are in the flexed conformation, HMM had a near zero ATPase activity while S-1 had a high ATPase rate (0.07 s-1). At 400 mM ionic strength, where both myosin and HMM are in the extended conformation, S1 and HMM had the same ATPase rate (0.04 s-1). Phosphorylation did not affect S1 significantly, but shifted the HMM curve to higher rates at lower ionic strengths. Both steady state and single turnover experiments gave the same results, indicating that steady state results were not skewed by multiple subfragment populations. These data indicate that HMM has a conformation-ATPase relation similar to that observed with myosin. Furthermore, these findings suggest that the S1 ATPase rate corresponds to that of HMM in the extended conformation. © 1993 Wiley-Liss, Inc.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970260404
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  • 6
    Digitale Medien
    Digitale Medien
    Three-dimensional organization of the platelet cytoskeleton during adhesion in vitro: Observations on human and nonhuman primate cells (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 589-608 
    Details
    ISSN: 0886-1544
    Schlagwort(e): platelet ; platelet adhesion ; cytoskeleton ; high voltage electron microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Adhesion of platelets in vitro resulted in rapid polymerization of the amorphous cytoplasmic ground substance into an organized cytoskeletal superstructure. This cytoskeleton, characterized through the use of whole-mount and stereo (3-D), high-voltage microscopy in conjunction with morphometrics and cytochemistry, comprised four major size classes of filaments organized in distinctive zones. The central matrix, or granulomere, at the center of the cell mass, was an ill-defined meshwork of 80-100-Å filaments which enshrouded granules, dense bodies, and elements of the dense tubular system as identified through peroxidase cytochemistry. Demarcasting this central matrix was a trabecular zone containing 30-50, 80-100, and 150-170 Å filaments in an open and rigid-appearing lattice. Circumscribing the trabecular zone and extending to the margins of the hyalomere was the third region, the peripheral web, in which 70-Å filaments were arranged in a tight honeycomb lattice. This organizational pattern was retained in cytoskeletons prepared by Triton x-100 extraction of the adherent cells, and was observed in basally located cells of aggregates which formed subsequent to adhesion. Our observations are consistent with biochemical studies of cytoskeletons prepared from suspended platelets and suggest a contractile protein composition for the superstructure during adhesion.
    Zusätzliches Material: 11 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cm.970030525
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  • 7
    Digitale Medien
    Digitale Medien
    Assessment of ram sperm mitochondrial function by quantitative determination of sperm rhodamine 123 accumulation (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 36 (1993), S. 354-360 
    Details
    ISSN: 1040-452X
    Schlagwort(e): Membrane potential ; Respiration ; Triton X-100 ; Fluorescence ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: A simple procedure is described for determining the functional state of ram sperm mitochondria by quantitative measurement of sperm rhodamine 123 (R 123) accumulation. Sperm were incubated with 1 μg/ml R 123, and the accumulated R 123 was measured fluorimetrically after release from washed sperm by detergent lysis. Ram sperm R 123 uptake was maximal after 30 min of incubation and responded to changes in both sperm (P 〈 0.01) and R 123 (P 〈 0.01) concentration. There was a linear relationship (r = 0.98) between R 123 uptake and the proportion of cold-shocked sperm present in a sperm sample. R 123 uptake was unaffected by 20 mM 2-deoxyglucose or by 10 mM malonate (the latter being sufficient to reduce O2 uptake; P 〈 0.01). R 123 accumulation in ram sperm was reduced by 6 mg/ml sodium pentobarbitone (P 0.05), by 1 μM 2,4-dinitrophenol (P 〈 0.01), and by 0.05% Triton X-100 (P 〈 0.01). It is concluded that quantitative estimation of R 123 uptake complements oxygen uptake in detecting mitochondrial dysfunction in ram sperm. While it is largely unaffected by inhibition of glycolysis, and is less sensitive than oxygen uptake to trichloroacetic acid cycle inhibition, R 123 uptake is sensitive to factors directly reducing the mitochondrial membrane potential of ram sperm. It may therefore be useful in the evaluation of the effects of such membrane-mediated injuries as cold shock and freezing damage on ram sperm mitochondria. © 1993 Wiley-Liss, Inc.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/mrd.1080360311
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  • 8
    Digitale Medien
    Digitale Medien
    Characterization of a cell surface glycoprotein associated with maturation of rat spermatozoa (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 37 (1994), S. 110-119 
    Details
    ISSN: 1040-452X
    Schlagwort(e): Sperm ; Glycoprotein ; GPI ; Maturation ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: The principal galactose oxidase/NaB[3H]4-labeled membrane protein of rat caudal epididymal spermatozoa was isolated by hydrophobic interaction chromatography. The protein is released from the membrane by the action of phosphatidylinositol specific phospholipase C, and thereby its properties are transformed from those of a protein anchored to the hydrophobic membrane to those of a hydrophilic solution protein. Because it is the only membrane-associated protein released by the enzyme which did not absorb to a propylaspartate resin, a simple, single step purification procedure was devised.Although the amino terminus of the protein is blocked to Edman degradation, the majority of the protein structure was determined from a series of tryptic peptides and from limited acid hydrolysis. Approximately 65% of the protein mass is carbohydrate which is primarily attached through O-glycosidic bonds to the 18 threonines. The molecular weight of the glycoprotein was estimated to be 16,600, considerably smaller than the Mr = 26,000 to 37,000 previously determined by gel electrophoresis. The anomalous electrophoretic behavior is undoubtedly due to the large percentage of carbohydrate. The distribution of carbohydrate on the protein side chains suggests the protein may form a positively charged, specialized scaffolding for the presentation of the carbohydrate moieties. Because the appearance of the ability to label the protein with galactose oxidase is correlated with sperm maturation in the epididymis, the glycoprotein structures may be an important componetn in the fertilization process. The combination of linkage by glycosylphosphatidylinositol and low molecular weight mucin-like structure indicates this may be a member of a new class of membrane proteins. © 1994 Wiley-Liss, Inc.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/mrd.1080370115
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  • 9
    Digitale Medien
    Digitale Medien
    Cell culture supports for slam-frozen and molecular distillation dried procedures (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 26 (1993), S. 184-185 
    Details
    ISSN: 1059-910X
    Schlagwort(e): Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Allgemeine Naturwissenschaft
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jemt.1070260215
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  • 10
    Digitale Medien
    Digitale Medien
    Enhanced in vitro growth of murine fibroblast cells and preimplantation embryos cultured in medium supplemented with an amphipathic peptide (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 31 (1992), S. 106-113 
    Details
    ISSN: 1040-452X
    Schlagwort(e): Embryo development ; Lytic peptide ; Growth factor ; Cecropin ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: Preliminary studies on the proliferative effects of lytic peptides were carried out using NIH 3T3 murine fibroblast cells and human lymphocytes. Cells were cultured in various concentrations of three different amphipathic peptides (SB-37, Shiva-1, and Vishnu), and enhanced proliferation was determined by uptake of 3Hthymidine with treated cells compared with control cultures. Enhanced proliferation of 3T3 cells was observed in cultures containing 50 μM or less SB-37. The primary study consisted of 263 four-cell- to eight-cell-stage mouse embryos from naturally bred mice and incubated in Whitten's medium containing 0.2, 1, or 10 μM of the amino terminus of an amphipathic cecropin B analog (Vishnu) or in Whitten's medium alone. Embryos were cultured to the hatched blastocyst stage, and effect of treatment was determined by the rate of growth to that stage of development. Statistical analysis revealed that culture in all three levels of Vishnu significantly accelerated in vitro growth of these stages of preimplantation embryos compared with controls. These results indicate that Vishnu promotes increased cleavage rates of embryos in vitro. A growth factor receptor clustering mechanism of action is proposed. This peptide may have some potential as an embryo culture medium additive to enhance in vitro growth rate.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/mrd.1080310204
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