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  • 1
    Electronic Resource
    Electronic Resource
    Separation of β-d-galactosidases in rabbit tissues: Genetics of neutral β-d-galactosidase (1983)
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    Details
    ISSN: 1573-4927
    Keywords: β-d-galactosidase ; β-d-glucosidase ; electrophoresis ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three different types of β-d-galactosidase (EC 3.2.1.23) could be distinguished in rabbit tissues using electrophoretic procedures. (1) Acid β-d-galactosidase with a low mobility and maximal activity at pH 3–5 was found in the particulate fraction of various tissue homogenates. This enzyme hydrolyzed 4-methylumbelliferyl-d-galactoside, but no activity against other glycoside substrates could be demonstrated. The enzyme was inhibited by galactono-(1 → 4)-lactone. (2) Lactose-hydrolyzing β-d-galactosidase with an intermediate mobility was found only in juvenile small intestine. Most of the activity was found in the particulate fraction of the cell. The enzyme hydrolyzed several other synthetic glycoside substrates besides lactose. It was most active at pH 5–6 and strongly inhibited by glucono-(1 → 5)-lactone but not much affected by galactono-(1 → 4)-lactone. (3) Neutral β-d-galactosidase with a fast mobility and maximal activity at pH 6–8 was found in the soluble fraction of homogenates from liver, kidney, and small intestine. This enzyme also showed a broad substrate specificity; it possessed activity against aryl-β-d-glucoside, -fucoside, and -galactoside substrates but not against lactose. The enzyme was strongly inhibited by glucono-(1 → 5)-lactone and (less) by galactone-(1 → 4)-lactone. Neutral β-d-galactosidase and neutral β-d-glucosidase (EC 3.2.1.21) are probably identical enzymes in the rabbit. Individual variation, in both electrophoretic mobility and activity, was found for neutral β-d-galactosidase. Genetic analysis of the electrophoretic variants revealed that two alleles at an autosomal locus are responsible for this variation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00000016
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Phase I and subsequent phase II study of filgrastim (r-met-HuG-CSF) and dose intensified cyclophosphamide plus epirubicin in patients with non-Hodgkin's lymphoma and advanced solid tumors (1999)
    Springer
    Annals of oncology 10 (1999), S. 907-914 
    Details
    ISSN: 1569-8041
    Keywords: cyclophosphamide ; dose-escalation ; epirubicin ; filgrastim ; G-CSF ; non-Hodgkin's lymphoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background: To define a maximum tolerated dose (MTD) for the combination of epirubicin and cyclophosphamide with filgrastim (r-met-HuG-CSF) in patients with advanced solid tumors and non-Hodgkin's lymphoma (NHL). Patients and methods: Thirty-five patients with advanced solid tumors were enrolled in stages I and II. Twenty-one patients were treated in stage I in sequential cohorts of at least three patients at increasing dosage levels of cyclophosphamide and epirubicin, for up to six cycles every 21 days. At the completion of stage I, a MTD for epirubicin was established. Fourteen patients were treated in stage II, in cohorts of three or more. The epirubicin dose remained constant at the MTD dosage from stage I. Cyclophosphamide was further dose-escalated to establish its MTD. Twenty-one patients with previously untreated non-Hodgkin's lymphoma were treated in stage III with the MTD established in the prior stages. Results: The MTD in stage I was epirubicin 150 mg/m2 and cyclophosphamide 1500 mg/m2 with cumulative neutropenia as the dose-limiting toxicity (DLT). Cumulative thrombocytopenia prevented further dose-escalation of cyclophosphamide in stage II. The stage III regimen consisted of six, 21-day cycles of epirubicin 150 mg/m2, cyclophosphamide 1500 mg/m2, vincristine 2 mg, and prednisolone 100 mg for five days with filgrastim support. Nineteen of twenty-one patients (90%) completed six cycles of treatment, eight (38%) without dose reduction. Common toxicity criteria (CTC) grade 4 neutropenia (neutrophil nadir 〈0.5 × 109/l) was documented in 85 of 118 cycles (72%). Neutropenic fever was documented in 17 of 21 patients (81%) on at least one occasion. Severe thrombocytopenia (〈25 × 109/l) was seen in fourteen of 118 cycles (12%) and increased with cycle number. There was no significant non-hematological toxicity. Conclusion: Significant dose-escalation of epirubicin and cyclophosphamide was possible with filgrastim support. The MTD achieved was approximately double that of standard-dose therapy. This study forms the basis of an ongoing randomized study evaluating dose-intensification in intermediate grade NHL.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008353522601
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  • 3
    Electronic Resource
    Electronic Resource
    Long-term survival advantage of MACOP-B over CHOP in intermediate-grade non-Hodgkin's lymphoma (1997)
    Springer
    Annals of oncology 8 (1997), S. 71-75 
    Details
    ISSN: 1569-8041
    Keywords: chemotherapy ; dose intensification ; long-term survival ; MACOP-B ; non-Hodgkin's lymphoma ; randomized trial
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background: The initial publication of the results of the Australianand New Zealand Lymphoma Group (ANZLG) randomized controlled trial comparingMACOP-B and CHOP in patients with intermediate-grade non-Hodgkin's lymphoma(NHL) showed equivalent complete response rates, time to treatment failure,and survival. Here we report the long-term follow-up of the 236 patientsentered on that study to determine if there were any long-term advantages ordisadvantages associated with MACOP-B. Patients and methods: Two hundred thirty-six eligible patients wererandomized between October 1986 and June 1991. The median duration offollow-up has been extended from 3.2 years in our previous publication to 6.5years. Results: As previously reported, the complete response (CR) rate forMACOP-B and CHOP chemotherapy was 51% and 59%, respectively. Theestimated failure-free survival rate for MACOP-B and CHOP patients was42% and 30%, respectively, at 5 years (P = 0.045) and37% and 25%, respectively, at 8 years (P = 0.057). Theestimated overall survival rate at 5 years was 54% for MACOP-B and41% for CHOP patients (P = 0.035) and at 8 years was 45%and 36%, respectively (P = 0.16). Conclusion: With this extended follow-up, we have shown a long-termsurvival advantage for MACOP-B chemotherapy over standard CHOP inpatients with intermediate-grade non-Hodgkin's lymphoma.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008262119154
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  • 4
    Electronic Resource
    Electronic Resource
    Genetics of a tissue esterase polymorphism (Est-6) in the rabbit (Oryctolagus cuniculus) (1987)
    Springer
    Biochemical genetics 25 (1987), S. 335-344 
    Details
    ISSN: 1573-4927
    Keywords: esterase ; genetics ; homology ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Genetic analysis of a polymorphic tissue esterase revealed a new locus (Est-6) with two alleles (Est-6 a andEst-6 b) on linkage group VI of the rabbit.Est-6 is closely linked to theEst-1,2,4 cluster. Esterase ofEst-6 is found in many organs, particularly in liver and small intestine, but not in erythrocytes and serum.Est-6 esterase hydrolyzes α-naphthyl acetate and butyrate, naphthol AS-D acetate, indoxyl acetate, and butyrate as well as 5-bromoindoxyl acetate,N-acetyl-l-alanine-α-naphthyl ester but not 4-methylumbelliferyl acetate and fluorescein diacetate. The enzyme is inhibited by bis-p-nitrophenyl phosphate and eserine but not byp-chloromercuribenzoate. It was classified as a carboxylesterase (EC 3.1.1.1). Based on chromosomal localization, tissue distribution, substrate specificity, inhibitor sensitivity, and range ofpI's, rabbitEst-6 is assumed to be homologous with mouseEs-7.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554543
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Separation of β-d-galactosidases in rabbit tissues: Genetics of neutral β-d-galactosidase (1983)
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    Details
    ISSN: 1573-4927
    Keywords: β-d-galactosidase ; β-d-glucosidase ; electrophoresis ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three different types of β-d-galactosidase (EC 3.2.1.23) could be distinguished in rabbit tissues using electrophoretic procedures. (1) Acid β-d-galactosidase with a low mobility and maximal activity atpH 3–5 was found in the particulate fraction of various tissue homogenates. This enzyme hydrolyzed 4-methylumbelliferyl-d-galactoside, but no activity against other glycoside substrates could be demonstrated. The enzyme was inhibited by galactono-(1 → 4)-lactone. (2) Lactose-hydrolyzing β-d-galactosidase with an intermediate mobility was found only in juvenile small intestine. Most of the activity was found in the particulate fraction of the cell. The enzyme hydrolyzed several other synthetic glycoside substrates besides lactose. It was most active atpH 5–6 and strongly inhibited by glucono-(1 → 5)-lactone but not much affected by galactono-(1 → 4)-lactone. (3) Neutral β-d-galactosidase with a fast mobility and maximal activity atpH 6–8 was found in the soluble fraction of homogenates from liver, kidney, and small intestine. This enzyme also showed a broad substrate specificity; it possessed activity against aryl-β-d-glucoside, -fucoside, and -galactoside substrates but not against lactose. The enzyme was strongly inhibited by glucono-(1 → 5)-lactone and (less) by galactone-(1 → 4)-lactone. Neutral β-d-galactosidase and neutral β-d-glucosidase (EC 3.2.1.21) are probably identical enzymes in the rabbit. Individual variation, in both electrophoretic mobility and activity, was found for neutral β-d-galactosidase. Genetic analysis of the electrophoretic variants revealed that two alleles at an autosomal locus are responsible for this variation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02395402
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Genetics of two tissue esterase polymorphisms (Est-4 and Est-5) in the rabbit (1983)
    Springer
    Biochemical genetics 21 (1983), S. 773-780 
    Details
    ISSN: 1573-4927
    Keywords: esterase ; polymorphisms ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two polymorphic esterase systems were found after electrophoresis of rabbit tissue homogenates. Each of these systems is controlled by an autosomal locus with two alleles. Est-4 determines the absence (Est-4a) or presence (Est-4b) of two bands of esterase activity with intermediate anodal mobility and broad substrate specificity. This polymorphism was found to be present in liver, small intestine, and spleen but not in kidney, heart, and testis. Est-5 is coding for cathodally migrating esterases which differ in mobility (Est-5a and Est-5b). This polymorphism was found only in kidney and testis homogenates. Est-5 esterases are more active against α-naphthyl acetate than against β-naphthyl acetate and have no activity against α-naphthyl butyrate. Linkage analysis indicated that Est-4 is localized on rabbit LG VI as part of a cluster of esterase loci, whereas Est-5 segregates independently. Rabbits from two inbred and nine partly inbred strains were tested for these polymorphisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498923
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    Paper (German National Licenses)
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