A study was conducted to determine the characteristics of the elderly who do not participate in health examinations, and to obtain basic health data on the elderly for developing a community health ...care plan. Elderly persons aged 60 or over who had not participated in mass health examinations in 1991 were interviewed regarding their conditions of activities of daily living (ADLs), and medical treatment, and their blood pressure was measured. Participation rate for health examinations in the elderly was 66%. Of the total 245 elderly who did not participate in health examinations, data from 215 (88%; 92 men and 123 women) were obtained. 1) The average age of the elderly who did not participate in health examinations was 3 years higher in men and 5 years higher in women than that of those who did participate (p < 0.01), and there were a larger number of persons aged 80 years or over. 2) The percentage of persons with a history of adult diseases such as cardiovascular disease was 63% which was 10% higher than those who participated in examinations (p < 0.01). 3) The percentage of persons requiring help in walking and/or mobility (13%) and bathing (10%) was higher than those who participated in examinations (p < 0.01). For seeing and hearing there were no differences between groups in the percentage of disabled persons. 4) There were more hypertensive people (> 160/95 mmHg) in those who did not participate in examinations (p < 0.01), but the percentage of the people who needed treatment (> 180/100 mmHg) was not different.(ABSTRACT TRUNCATED AT 250 WORDS)
The nucleotide sequence of the import precursor of coupling factor 6 (factor 6) of rat liver H(+)-ATP synthase has been determined from a recombinant cDNA clone isolated by screening a rat liver cDNA ...library with a probe DNA. The sequence was composed of 458 nucleotides including a coding region for the import precursor of factor 6 and noncoding regions of both the 5'- and 3'-sides. The import precursor of factor 6 and its mature polypeptide deduced from the open reading frame consisted of 108 and 76 amino acid residues with a molecular weight of 12,494 and 8,927, respectively. The presequence of 32 amino acids could be the import signal peptide which serves to direct the protein into the mitochondrial matrix.
The frequency of the ring-breathing (Ca-Cm stretching) Raman line of bacteriochlorophyll a (BChl) in the T1 state was determined in 16 different solvents. The ring-breathing vibration in the T1 state ...frequencies were in the region of 1578-1581 cm-1 in polar solvents forming the hexa-coordinated monomers, while they were in the region of 1585-1591 cm-1 in polar solvents forming the penta-coordinated monomers. The ring-breathing vibration in the T1 state frequencies were 1597 and 1599 cm-1 in methylene chloride and carbon tetrachloride forming penta-coordinated BChl aggregates. Possible mechanisms in which the ring-breathing vibration in the T1 state frequency reflects the states of intermolecular interactions are discussed. The ring-breathing vibration in the T1 state frequency of BChl that was bound to the light-harvesting complex (LHC) of Rhodobacter sphaeroides R26 was found to be 1598 cm-1, a result which suggests that a pair of BChl molecules form a dimer in the LHC in the T1 state.
Peroxidase was prepared from extracts of barley leaves and separated into seven components, different in pI. The purification procedure comprised two parts. The first part was based on the fact that ...all the components had practically the same molecular weights. It consisted of fractionations with acetone and ammonium sulfate, ion-exchange chromatographies on CM-cellulose and DEAE-Sepharose CL-6B, and molecular-sieve chromatography on Ultrogel AcA44; the components were all purified together to near homogeneity on sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis, and the procedure resulted in 1,200-fold puri fication with a yield of 39%. The ion-exchange chromatographies were carried out under conditions such that the components would not be adsorbed. In the second part, the enzyme preparation was separated into the seven components by repeating isoelectric electrophoresis. Their isoelectric points (pI) were 6.3, 6.8, 7.4, 8.3, 8.5, 8.7, and 9.3. The components other than the pI 6.3 and 6.8 components were each purified to homogeneity in the electrophoresis. The seven components thus prepared were the same in molecular weight on SDS-gel electrophoresis (44,000) and showed absorption maxima at the same wave lengths (403, 496, and 534 nm), RZ (A403/A375) ranging from 2.09 to 2.81. Their protoheme IX contents were 0.81–1.07 mol/mol, and their true sugar contents 15–26% (g/g). The amino acid compositions suggest that the five components described above are not real isoenzymes, but exhibit different pI values due to differences in glycosyl residue. The pI 9.3 component was crystallized in spite of its high sugar content.
We report here on electrochemical ion chromatography using glassy carbon powders modified with polyaniline. Separation in this technique is based on the insertion of anions into a polymer film in its ...oxidized states. Thus, the separation of anions can be controlled by changing the potential of the film electrochemically; the retention time of the anions increased with an increase in the potential. Separation was optimized by changing the pH of the mobile phase and column length.
With Rhodospirillum rubrum, hydrogenase was found to exist partly as an extracellular enzyme in the culture medium. After 4-day cultivation, the total activity and the specific activity of the enzyme ...in the medium were about 10 times and 230 times as high as those in the crude extract obtained from disrupted cells. The time course for the production of hydrogenase during cultivation was studied.
An HPLC assay for determination of ATPase activity was developed and validated. After stopping the enzyme reaction of the enzyme source (rat renal cortical basolateral membranes) with ATP, products ...derived from ATP were analyzed by two methods; HPLC determination of ADP derived from ATP, and colorimetry of inorganic phosphorus (P
i) released from ATP. This HPLC procedure was precise and linear over the range of protein amount of the enzyme source studied, and the intra- and inter-assay variations were lower than 10%. The values that were obtained by the two methods revealed a significant correlation. Also, even when the samples contained P
i or were contaminated with P
i, this HPLC method allowed determination of ATPase activity. In addition, when ouabain was used as an inhibitor, the HPLC method was found to be applicable for Na,K-ATPase determination. This indicated that this HPLC assay would enable determination of ATPases other than Na,K-ATPase, when other inhibitors are employed instead of ouabain.
DNA polymerase A (I or major) and its stimulative factor were purified from 15–20 kg wet weight of baker's yeast by several procedures, which were varied in order to examine the possible occurrence ...of proteolysis. The extraction was carried out in the presence of 10 or 3 mM phenylmethylsulfonyl fluoride (PMSF), followed by either batchwise adsorption-elution or column chromatography on DEAE-Sepharose (rapid or time-consuming, respectively). These early steps were followed by column chromatographies on DEAE−, CM−, and heparin-Sepharoses, phosphocellulose, and Sephacryl S-300. Preparations of the polymerase obtained by all the procedures described above showed a single protein band at Mr of about 145,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), unless they had been treated with 2-mercaptoethanol (ME). After ME treatment, however, they showed two protein bands at Mr of about 145,000 and 75,000 in SDS-PAGE, except - for those obtained by the procedure involving 10 mM PMSF and the batchwise adsorption-elution. All the preparations described above showed practically the same specific activity. This indicates that in intact cells, the polymerase consisted of a single peptide with Mr of about 145,000, and that after cell disruption, it was artificially hydrolyzed in a limited fashion into two peptides with Mr of about 75,000, which were still active and were linked to each other through a disulfide bond. Preparations of the factor obtained by all the procedures described above showed a single protein band at Mr of about 20,000 in SDS-PAGE before and after ME treatment. The relative activities of the purified polymerase were (100%), 123, 21,37,196, and 38% with native and denatured salmon sperm DNA, native and denatured calf thymus DNA, poly(dA-dT), and poly(dA0).ologio(dT)10, respectively. With the addition of the purified factor, they were 173,272,173,217,173,and 247% respectively, i.e., significantly stimulated. The purified factor also stimulated the activity of calf thymus DNA polymerase α by 150% with denatured salmon sperm DNA; km was about 5 ×10−10M, practically the same as that of yeast DNA polymerase A. However, it hardly influenced the activities of Escherichia colienzyme I or Micrococcus luteus enzyme.
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