Rinsho Ketsueki
Online ISSN : 1882-0824
Print ISSN : 0485-1439
ISSN-L : 0485-1439
Volume 14, Issue 4
Displaying 1-14 of 14 articles from this issue
  • Mitsuo KOZURU
    1973Volume 14Issue 4 Pages 480-487
    Published: 1973
    Released on J-STAGE: October 31, 2008
    JOURNAL RESTRICTED ACCESS
    1) In 87 of clinical cases, the ratio of T I B C to immunochemically determined transferrin level was 1.29±0.028μg of iron per milligram of transferrin.
    2) Five cases of congenital atransferrinemia were reviewed and the function of transferrin was discussed from the hematological points of view.
    3) Genetic variants of transferrin was determined by starch gel electrophoresis. Five cases of TfBC and 20 cases of TfCD were found in 1950 of clinical cases. These genetic variants, however, possessed normal iron binding capacity.
    4) The turnover rate of human transferrin was investigated and the following date were obtained by means of Mathew's method in 8 normal subjects.
    Half time 10.2±1.11 days
    Metabolic Pool 266±75.1 mg/kg
    Catabolic Rate 14.9±3.03 %/day
    Synthetic Rate 21.4±6.08 mg/kg/day
    The cases of iron deficiency anemia exhibited a longer half time than normal controls. In contrast, the cases of primary hemochromatosis and hemosiderosis showed a shorter half time than normal controls.
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  • Takehiko SASAZUKI
    1973Volume 14Issue 4 Pages 488-494
    Published: 1973
    Released on J-STAGE: October 31, 2008
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    The concept that haptoglobin is a specific antibody to hemoglobin is a prominent hypothesis in suggesting ways to investigate the true physiological role of haptoglobin. Accepting the notion that organisms produce antibody directed against a foreign substance in order to remove it more efficiently, an attractive working hypothesis is that haptoglobin serves the same purpose with respect to hemoglobin.
    When comparing the immunochemical properties of haptoglobin with those of antihemoglobin antibody, however, there are many differences between them (precipitation reaction, complement fixation reaction, and binding site and binding mechanisms with hemoglobin).
    Further comparison of physicochemical properties of hemoglobin associated with haptoglobin and that of hemoglobin associated with specific anitibody also revealed many differences (oxygen affinity, peroxidase activity, resistance to acid denaturation, absorption spectra, susceptibility of heme to sodium hydrosulfite, and conformation around heme).
    Although, as outlined above, haptoglobin and immunoglobulin, as well as hemoglobin-haptoglobin complex and hemoglobin-antihemoglobin antibody complex differ in several significant immunological and physicochemical properties which in turn affect their respective incorporation and metabolism by organisms, and haptoglobin cannot be recognized as a specific antibody to hemoglobin in common sence, nevertheless, similarities in structure and biological roles are close enough to warrant further investigations along these lines in the hope of clarifying their respective biological functions in the organism.
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  • Tatsuo SEZAKI
    1973Volume 14Issue 4 Pages 495-501
    Published: 1973
    Released on J-STAGE: October 31, 2008
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  • [in Japanese]
    1973Volume 14Issue 4 Pages 502-506
    Published: 1973
    Released on J-STAGE: October 31, 2008
    JOURNAL RESTRICTED ACCESS
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  • [in Japanese]
    1973Volume 14Issue 4 Pages 507-513
    Published: 1973
    Released on J-STAGE: October 31, 2008
    JOURNAL RESTRICTED ACCESS
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  • Nobuo TANAKA
    1973Volume 14Issue 4 Pages 514-519
    Published: 1973
    Released on J-STAGE: October 31, 2008
    JOURNAL RESTRICTED ACCESS
    The determination of serum B12 concentration, unsaturated B12 binding capacity, separaption of transcobalamin 1 and transcobalamin 11, measurement of endogenous B12 in transcobalamins and investigation of natural occurrence of B12 derivatives in serum and transcobaiamins were done on sera from healthy individuals, patients with chronic granulocytic leukemia and acute hepatitis.
    Methylcobalamin (CH3-B12) in serum and transcobalamin 1 from healthy individuals, chronic granulocytic leukemia and acute hepatitis patients were found as the major form of occurrence, but dimethylbenzimidazolylcobamide coenzyme (DBCC) and hydroxocobalamin (OH-B12) were slightly increased in serum and transcobalamin 1 from chronic granulocytic leukemia and acute hepatitis as compared with those from healthy individuals.
    In transcobalamin 11 the proportion of occurrence of OH-B12, DBCC, and CH3-B12 was considerably similar, but DBCC was relatively increased in transcobalamin 11 from acute hepatitis patients, suggesting that it is due to a release of DBCC from the liver.
    Comparing the activities of 57Co in transcobalamins from sera of rats administered intracutaneously with 50 ng of CH3-B12-57Co, DBCC-57Co and CN-B12-57Co two hours before separating transcobalamins, there were no statistically significant differences in the uptake of cobalamins between transcobalamin 1 and transcobalamin 11.
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