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  • 1
    Publication Date: 2021-05-19
    Description: Published
    Repository Name: AquaDocs
    Type: Journal Contribution , Refereed
    Format: pp.115-120
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  • 2
    Publication Date: 2021-05-19
    Description: Published
    Repository Name: AquaDocs
    Type: Journal Contribution , Refereed
    Format: pp.119-125
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 25 (1992), S. 470-474 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 25 (1992), S. 475-478 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4919
    Keywords: bone metabolism ; β-alanyl-L-histidinato zinc ; proliferative effect ; protein synthesis ; osteoblastic cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of β-alanyl-L-histidinato zinc (AHZ) on bone metabolism was investigated in osteoblastic MC3T3-El cells. Cells were cultured for 3 days at 37°C in a CO2 incubator in plastic dishes containing α-modified minimum essential medium supplemented with 10% fetal bovine serum. After the cultures, the medium was exchanged for that containing 0.1% bovine serum albumin plus various concentrations of AHZ or other reagents, and the cells were cultured further for appropriate periods of time. The presence of AHZ (10−7–10−5M) stimulated the proliferation of cells. AHZ (10−6 and 10−5M) increased deoxyribonucleic acid (DNA) content in the cells with 48hr-culture. This increase was completely blocked by the presence of cycloheximide (10−6M) or hydroxyurea (10−3M). Also, the presence of cycloheximide (10−6M) completely inhibited the AHZ (10−5M)-induced increase in the proliferation of cells. Meanwhile, parathyroid hormone (10−7M), estrogen (10−9M) and insulin (10−M) significantly increased cellular DNA content. However, these hormonal effects clearly lowered in comparison with that of AHZ (10−5M). Dibutyryl cyclic AMP (10−4M) and zinc sulfate (10−5M) did not cause a significant increase in cellular DNA content. The present results support the view that AHZ has a direct specific proliferative effect on osteoblastic cellsin vitro and that this effect is dependent on protein synthesis.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 122 (1993), S. 65-68 
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; tissue concentration ; liver ; kidney ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The concentration of calcium-binding protein regucalcin in the tissues of rats was estimated by enzyme-linked immunoadsorbent assay (ELISA) with rabbit-anti-regucalcin IgG. In male rats (5 weeks old), regucalcin was most pronounced in the liver. Liver regulcalcin concentration was about 0.1μM, when it was calculated with regucalcin molecular weight of 28,800. The relatively higher level of regucalcin was also found in the kidney as compared with that of the skeletal muscle, duodenum, testis, lung, heart, spleen, cerebral cortex and hippocampus. Similarly in female rats, regulacalcin was remarkable in the liver, and appeared only slightly in the kidney. Thus, the tissue distribution of regucalcin in rats was specific in the liver. The concentration of regucalcin in the liver was altered with increasing age of rats; liver regucalcin level linearly increased during 5 weeks old after birth of male rats, and then began to decrease gradually. The results coincided with the previous observation of Northern blot analyses by using liver regucalcin cDNA as a probe. The present finding clearly demonstrates that regucalcin is specifically synthesized in the liver of rats.
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  • 7
    ISSN: 1573-4919
    Keywords: regucalcin ; calcium-binding protein ; (Ca2+−Mg2+)-ATPase ; plasma membrane ; rat liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of various metals and regucalcin, a calcium-binding protein isolated from rat liver cytosol, on (Ca2+−Mg2+)-ATPase activity in the plasma membranes of rat liver was investigated. Of various metals (Zn2+, Cu2+, Ni2+, Mn2+, Co2+ and Al3+; 100 μM as a final concentration), Mn2+ and Co2+ increased markedly (Ca2+−Mg2+)-ATPase activity, while other metals had no effect. When Ca2+ was not added into enzyme reaction mixture, Mn2+ and Co2+ (25–100 μM) did not significantly increase the enzyme activity, indicating that heavy metals act on Ca2+-stimulated phosphorylation of the enzyme. Meanwhile, regucalcin (0.25–1.0 μM) caused a remarkable elevation of (Ca2+−Mg2+)-ATPase activity. This increase was not inhibited by the presence of 100 μM vanadate, although the effects of Mn2+ and Co2+ (100 μM) were inhibited by vanadate. Also, the inhibition of the Mn2+ and Co2+ effects by vanadate was not seen in the presence of regucalcin. Moreover, regucalcin (0.5 μM) increased significantly the enzyme activity in the absence of Ca2+. This effect of regulcalcin was not altered by increasing concentrations of Ca2+ added, indicating that the regucalcin effect does not depend on Ca2+. The present results suggest that regucalcin activates directly (Ca2+−Mg2+)-ATPase in liver plasma membranes, and that the activation is not involved in the Ca2+-dependent phosphorylation of the enzyme.
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  • 8
    ISSN: 1573-4919
    Keywords: β-alanyl-L-histidinato zinc ; bone metabolism ; cell differential effect ; protein synthesis ; osteoblastic cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effect of β-alany-L-histidinato zinc (AHZ) on bone cell function was investigated in osteoblastic MC3T3-E1 cells. Cells were cultured for 3 days at 37°C in a CO2 incubator in plastic dishes containing α-modified minimum essential medium supplemented with 10% fetal bovine serum. After the cultures, the medium was exchanged for that containing 0.1% bovine serum albumin plus AHZ (10−7–10−5 M) or other reagents, and the cells were cultured further for appropriate periods of time. The presence of AHZ (10−7–10−5 M) produced a remarkable increase of alkaline phosphatase activity and protein concentration in osteoblastic cells. Thus increases were seen with the prolonged cultivation (12–21 days). With the culture of 1, 3 and 12 days, the effect of AHZ (10−6 M) to increase alkaline phosphatase activity and protein concentration was more intensive than the effect of zinc sulfate, (10−6 M). The AHZ effects were completely abolished by the presence of cycloheximide (10−6 M), indicating that AHZ stimulates protein synthesis in the cells. The present study suggests that AHZ has a stimulatory effect on cell differentiation, and that this effect is partly involved on protein synthesis in osteoblastic cells.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 131 (1994), S. 167-172 
    ISSN: 1573-4919
    Keywords: Ca2+-ATPase ; Ca2+ transport ; Ca2+ channel ; rat liver nuclei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The regulatory role of Ca2+-stimulated adenosine 5′-triphosphatase (Ca2+-ATPase) in Ca2+ transport system of rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+-ATPase activity was calculated by subtracting Mg2+-ATPase activity from (Ca2+−Mg2+)-ATPase activity. The release of Ca2+ from the Ca2+-loaded nuclei was evoked progressively after Ca2+ uptake with 1.0 mM ATP addition, while it was only slightly in the case of 2.0 mM ATP addition, indicating that the consumption of ATP causes a leak of Ca2+ from the Ca2+-loaded nuclei. The presence of N-ethylmaleimide (NEM; 0.1 mM) caused an inhibition of nuclear Ca2+ uptake and induced a promotion of Ca2+ release from the Ca2+-loaded nuclei. NEM (0.1 and 0.2 mM) markedly inhibited nuclear Ca2+-ATPase activity. This inhibition was completely blocked by the presence of dithiothreitol (DTT; 0.1 and 0.5 mM). Also, DTT inhibited the effect of NEM (0.1 mM) on nuclear Ca2+ uptake and release. Meanwhile, verapamil and diltiazem (10 μM), a blocker of Ca2+ channels, did not prevent the NAD+ (1.0 and 2.0 mM), zinc sulfate (1.0 and 2.5 μM) and arachidonic acid (10 μM)-induced increase in nuclear Ca2+ release, suggesting that Ca2+ channels do not involve on Ca2+ release from the nuclei. These results indicates that an inhibition of nuclear Ca2+-ATPase activity causes the decrease in nuclear Ca2+ uptake and the release of Ca2+ from the Ca2+-loaded nuclei. The present finding suggests that Ca2+-ATPase plays a critical role in the regulatory mechanism of Ca2+ uptake and release in rat liver nuclei.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 117 (1992), S. 153-158 
    ISSN: 1573-4919
    Keywords: bone protein ; zinc ; estrogen ; insulin ; rat calvaria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract An attempt was made to clarify the molecular characterization of zinc-induced bone protein synthesis in tissue culture. Calvaria were removed from weanling rat (3-week-old male) and cultured for periods up to 48 hr in Dulbecco's Modified Eagle Medium (high Glucose, 4500 mg/dl) supplemented with antibiotics and bovine serum albumin. When calvaria cultured in the presence of 10−5 to 10−4 M zinc were pulsed with [3H] leucine, zinc caused a significant increase in the incorporation of [3H] leucine into the acid-insoluble residues of bone tissue. The soluble fraction obtained from cultured bone was analyzed with SDS-polyacrylamide gel electrophoresis (SIDS-PAGE). The major components in the fraction obtained from control bone were 68 killo-dalton (kDa) and 45 kDa proteins. These components were clearly increased by the presence of zinc (10−4 M). The effect of zinc was completely abolished by the coexistence of 10−6 M cycloheximide. Meanwhile, 10−9 M estrogen or 10−8 M insulin, which can stimulate bone formation, did not enhance the effect of zinc to increase bone 68 and 45 kDa proteins. The present findings suggest that zinc increases many bone protein components, especially 68 and 45 kDa proteins.
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