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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 34 (1978), S. 3233-3237 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 34 (1978), S. 1283-1286 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 35 (1979), S. 2033-2037 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 33 (1977), S. 2550-2553 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-0827
    Keywords: Bone mineral ; Calciphylaxis ; Calcinosis ; ESR ; Free radicals
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The evolution of the mineral constituents of subcutaneous calcinosis induced in rats by topical calciphylaxis was studied by the method of quantitative chemical analysis, and after treatment with excited gases by electron spin resonance (ESR) analysis. Chemical data show that the genesis of the subcutaneous calcinosis does not significantly alter the concentration of Ca, P, F, CO3, Mg, and Fe in the mineral phase of the femoral bone of calciphylactic rats. In the calcinosis an important increase of the fluoride concentration is noticed in function of the time after challenging. There is also a high concentration of Mg2+ ions in the early stages of the experimental calcification. Iron injected for the challenging is continuously present in the calciphylactic tissue after this treatment. This suggests that subcutaneous calcinosis might be a means of fixing certain heavy metal ions. After treatment with excited gases, the proportions of the trapped CO3 3− and O3 − radicals are of the same order of magnitude in calciphylactic tissue after 12 days and observations in bone mineral. These suggest that after 12 days the mineral of the calciphylactic tissue has a crystalline state close to that of bone.
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  • 6
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A new deficient G-6PD variant, Gd(-) Abrami, was found in granulocytes, platelets and red blood cells of a 65-year-old woman with myelofibrosis. Enzyme and immunological titrations showed that only the deficient variant was present in blood cells whereas both the normal and abnormal enzymes were found in the fat cells of this patient. These results seem to indicate that the granulocytes, platelets and erythrocytes of this woman with myelofibrosis have arisen from a single abnormal precursor the functional X chromsome of which is the one carrying the abnormal G-6PD gene.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Human genetics 〈Berlin〉 31 (1976), S. 83-91 
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A case of hereditary nonspherocytic hemolytic anemia associated with partial erythrocyte PFK deficiency without muscular symptoms is reported: erythrocyte enzyme activity in the propositus was 60% of normal. Kinetic studies of erythrocyte PFK revealed increased sensitivity to ATP inhibition and decreased sensitivity to citrate inhibition. Muscle PFK from the patient had a normal enzymatic activity, but was highly unstable to heat, dilution without stabilizer and urea; furthermore its starch gel electrophoretic mobility was markedly faster than the one of a normal control. The results suggested that a muscle type's subunit was deficient in the erythrocyte PFK. The authors hypothesize that there was no PFK deficiency in the patient's muscle because of the active synthesis of proteins by this tissue. In contrast, the deficiency of PFK would be easily detected in erythrocytes, because of the absence of protein synthesis.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Human genetics 〈Berlin〉 33 (1976), S. 35-46 
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary By focusing in sucrose, gradient L-type pyruvate kinase from human liver could be separated into 2 major forms (pI 6.28±0.03 and 5.85±0.09) and a minor more acid form (pI≙5). These different forms could also be detected by focusing in acrylamide-ampholine slab gel. The major forms were interconvertible, the equilibrium being shifted toward the acid form by fructose 1,6-diphosphate and SH reagents, and toward the alkaline form by proteinic factors extracted by ammonium sulphate fractionation from liver extracts and from hemolysates. These factors seemed to be responsible for the stabilization of the liver crude extract enzyme in its alkaline conformation. By acrylamide slab gel electrofocusing, erythrocyte pyruvate kinase from whole hemolysates exhibited a complex pattern composed of at least 3 interconvertible forms. The in vitro aging of the red blood cells and the storage of the hemolysates resulted in a progressive disappearance of the acid forms and in a strengthening of the alkaline form. Partially purified erythrocyte enzyme focused in 2 major bands, interconvertible under the influence of the same factors as those described for L-type pyruvate kinase. Although closely related, the focusing patterns of L-type and erythrocyte-type were never exactly identical. Double immunodiffusion against antihuman L-type serum showed a complete identity reaction between erythrocyte-and L-type pyruvate kinases. Moreover, antihuman M2-type serum was unable to neutralize erythrocyte pyruvate kinase as well as to change its electrophoretic mobility. Consequently, we conclude that both human erythrocyte-and liver L-type pyruvate kinases existed under several conformers interconvertible under the influence of the same ligands or proteinic factors; erythrocyte-type enzyme seems to include L-type subunit and not M1- or M2-type subunits. The erythrocyte- and L-type enzymes, however, are not identical and the nature of the differences between them is discussed.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Human genetics 〈Berlin〉 31 (1976), S. 35-45 
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Anti human M2 type and anti human L type pyruvate kinase sera allowed us to distinguish two groups of pyruvate kinase in man. Erythrocyte and liver (L type) enzymes on the one hand were inhibited by anti L and not at all by anti M2 serum; pyruvate kinase from all the other tissues on the other hand were inhibited by anti M2 and not at all by anti L serum. This latter group represent the M type pyruvate kinase isozymes. The M type isozymes have been studied by electrofocusing in thin layer acrylamideampholine gel. In adult tissues 4 types of isozymes were found, designated, from acid to alkaline pH, as M2 (predominant form in spleen, leukocytes, lung...), M3, M4 and M1 (predominant form in muscle and brain). In foetal tissues an extra band M2, called M2f, more anodic than M2, was added to the previously described isozymes. Except in brain (in which the isozymes M2, M3, M4 and M1 were found), the most anodic bands (M2f, M2 and M3) were predominant in all the foetal tissues. The isozymes M2f and M2 seem therefore to be the original M type pyruvate kinase forms from which the other isozymes issue. The rate of each isozyme seems to depend on tissue factors characterizing the state of differentiation of some tissues, as indicated by the ability of adult muscle extracts to change the isozymes M2 and M3 into more cathodic forms.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Human genetics 〈Berlin〉 29 (1975), S. 271-280 
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Erythrocyte pyruvate kinase (PK) from 5 patients with congenital non-spherocytic hemolytic anemia and erythrocyte PK deficiency have been studied by immunological methods and electrofocusing. L type immunologically related PK was titrated in crude hemolysate with anti human liver L type PK rabbit serum and M2 type immunologically related PK with anti human leukocyte M2 type PK serum. After partial purification, molecular specific activity of erythrocyte PK was measured by immunoinactivation and electroimmunodiffusion with anti L type PK serum. Partially purified erythrocyte PK was focused on continuous sucrose gradient with 2% ampholines covering the pH range 5–8. PK enzymatic deficiency was due two times to a lowered molecular specific activity of the PK variants, the concentration of PK antigen being in the normal range. In the 3 other cases enzyme activity and immunological reactivity were likewise lowered. In the 2 patients with the most marked erythrocyte PK deficiency about 50% of the residual activity in crude hemolysate were non inhibited by anti L type PK serum, but were inhibited by anti M2 type PK serum. In 3 patients, the electrofocusing pattern of partially purified PK was significantly different from that of normal controls. In conclusion, the heterogeneity of the molecular mechanisms of the deficiency on the one hand, and the abnormalities of electrofocusing patterns on the other hand, seem to indicate that erythrocyte PK deficiency is due to the synthesis by muted structural genes of various abnormal PK molecules. The high ratio of M2 type PK in the most deficient hemolysates may be due to a compensatory process.
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