Relation between use of health check ups starting in middle age and demand for inpatient care by elderly people in Japan.

OBJECTIVE--To find out whether there is any correlation between the use of general health check ups (provided for by the Health Services for the Elderly Act 1982) by insured Japanese residents aged 40 or older and demand by the elderly for inpatient care. DESIGN--A questionnaire was posted in 1988 to municipal offices of Japanese cities. All questionnaires were returned with data for 1983 and 1986. SETTING--All 509 Japanese cities with a population of 30,000-199,999. SUBJECTS--All people aged 40 or older who hold a resident card and are not offered health examinations at work are eligible for general health check ups. The questionnaire also inquired about use of inpatient care by elderly residents (aged 70 or older) who were covered by national health insurance. MAIN OUTCOME MEASURES--Correlation coefficients between the rates of use of general health check ups and mean annual bed days for the elderly. Comparison of relative changes by analysis of correlation between improvement indices in mean bed days and mean inpatient fee. RESULTS--In cities with relatively high rates of use of health check ups both the mean annual bed days and the mean inpatient fee for the elderly tended to be low. Correlation coefficients between the logarithmic rates of use of check ups and mean bed days by sizes of cities and number of beds were all negative values. There tended to be more correlation between improvement indices for rate of use of check ups and both mean bed days and mean inpatient fee with higher rates of use in 1983, and the correlation was significant for rates of 60% or more. CONCLUSIONS--Strong health service programmes that start in middle age decrease the demand for inpatient care of the elderly. It was estimated that in a single year from 1985 to 1986, when there was an increase in the rate of use of check ups from 25.5% to 27.6%, the reduction in the number of bed days for the total of 8.5 million elderly insured people was 2.21 million bed days.     

Protective effect of anti-anxiety drugs against hypoxia

The effect of psychotropic agents was studied on the survival of mice subjected to hypoxia. A significant prolongation of the survival time was observed in the animals pretreated with anti-anxiety drugs. However, anti-psychotic drugs or thymoleptics failed to exert such elongation effect under the same condition. The order of potency on anti-hypoxia activity was: Y-6047 = diazepam = nitrazepam > oxazapem > chlordiazepoxide > medazepam, namely in the ratio of 30 : 10 : 3 : 1, approximately. A relationship between anti-anxiety activity and anti-hypoxia activity is also discussed.     

Affinity chromatography of Aspergillus acid proteinase on an N,O-dibenzyloxycarbonyl-tyrosine-AH-Sepharose 4B column

N,O-dibenzyloxycarbonyl-l-tyrosine Z-Tyr(Z) has been found to be a specific inhibitor of Aspergillus acid proteinase and was coupled with hexamethylene-diamino-Sepharose 4B (AH-Sepharose 4B). By affinity chromatography employing a Z-Tyr(Z)-AH-Sepharose 4B column, acid car?ypeptidase-free Aspergillus acid proteinase was obtained.     

N-acetylgalactosamine 4,6-bissulfate in rat urine I. Isolation, identification and chemical synthesis

By starting with 4 l of rat urine, it was possible to obtain a sulfate ester of hexosamine in crystalline form. A series of identification procedures including chemical analyses, enzymatic digestion, proton magnetic resonance spectroscopy and infrared spectroscopy showed that this substance is 2-acetamido-2-deoxy-D-galactose 4,6-bissulfate. The trivial name for this compound is N-acetylgalactosamine 4,6-bissulfate; structural formula:

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Quantitation by isotopic techniques indicated the urine possessed an average concentration of 8 μM N-acetylgalactosamine 4,6-bissulfate.Further extension of these studies necessitated the chemical synthesis of N-acetylgalactosamine 4,6-bissulfate and related compounds to be used for references or as biological substrates. Direct sulfation of N-acetylgalactosamine was attempted first, and strong preference for attak on the primary hydroxyl group (position 6) was found for chlorosulfonic acid. Thus, the reaction with 2.2 molar equivalents of the sulfating agent gave N-acetylgalactosamine 6-sulfate and its derivatives bearing a second sulfate at either position 1 (minor) or position 3 (major). The lack of sulfation at position 4 could be attributed to steric effects of the sulfate group preferentially attached to position 6. Another experiment in which UDP-N-acetylgalactosamine 4-sulfate was used in place of the free sugar led to the formation of a bissulfated sugar-nucleotide which, on subsequent hydrolysis with mild acid, afforded N-acetylgalactosamine 4,6-bissulfate, the same compound as that obtained from rat urine.     

Alpha-lactalbumin as a lysosomal enzyme-releasing factor

In the early stage of mammary gland involution, biochemically detectable lysosomal damage occurs. The mechanism(s) underlying this damage is not well understood. We found that alpha-lactalbumin from mouse milk induced the release of enzymes from the lysosomes of mouse mammary epithelial cells in vitro, and this induction also occurred with bovine alpha-lactalbumin. This enzyme release was accelerated by the addition of whey proteins with a molecular weight of 50 000 to 60 000. We also found that the lysosomal membrane of mammary epithelial cells had a strong affinity for alpha-lactalbumin.     

Comparative studies on multiple forms of serum cholinesterase in various species

Multiple forms of serum cholinesterase (ChE) were compared in 8 species by electrophoretic technique and the following characteristics were noted. The first moving fraction markedly hydrolyzed butyrylthiocholine and the activity was not inhibited by 10(-5)M eserine in the serum of some rabbits tested. Electrophoretic patterns of the ChE were obtained by use of two thiocholines as substrate, and the number of fractions against acetylthiocholine were more than against butyrylthiocholine in dogs, miniature pigs, rabbits, and hamsters. The activities of ChE fractions of dogs (C3), miniature pigs (C1, C2), rabbits (C1), and hamsters (C3) were inhibited by 6.1 X 10(-2)M caffein but not by 10(-4)M ethopropazine, which suggests that the fractions are all true-ChE.     

Oxidative inactivation of an extramitochondrial acetyl-CoA hydrolase by autoxidation of L-ascorbic acid

The activity of acetyl-CoA hydrolase (dimeric form) purified from the supernatant fraction of rat liver was shown to have a half-life (t1/2) of 3 min at 0 degree C, but to stable at 37 degrees C (t1/2 = 34 h) [Isohashi, F., Nakanishi, Y. & Sakamoto, Y. (1983) Biochemistry 22, 584-590]. Incubation of the purified enzyme with L-ascorbic acid (AsA) at 37 degrees C resulted in inactivation of the enzyme (t1/2 = 90 min at 2 mM AsA). The extent of inactivation was greatly enhanced by addition of transition metal ions (Cu2+, Fe2+, and Fe3+). Thiol reducing agents, such as reduced glutathione and DL-dithiothreitol, protected the hydrolase from inactivation by AsA. However, these materials did not restore the catalytic activity of the enzyme inactivated by AsA. When AsA solution containing Cu2+ was preincubated under aerobic conditions at 37 degrees C for various times in the absence of enzyme, and then aliquots were incubated with the enzyme solution for 20 min, remaining activity was found to decrease with increase in the preincubation time, reaching a minimum at 60 min. However, further preincubation reduced the potential for inactivation. Catalase, a hydrogen peroxide (H2O2) scavenger, almost completely prevented inactivation of the enzyme by AsA plus Cu2+. Superoxide dismutase and tiron, which are both superoxide (O2-) scavengers, also prevented inactivation of the enzyme. A high concentration of mannitol, a hydroxyl radical (OH) scavenger, partially protected the enzyme from inactivation. These results suggest that inactivation of the enzyme by AsA in the presence of Cu2+ was due to the effect of active oxygen species (H2O2, O2-, OH) that are known to be autoxidation products of AsA. Valeryl-CoA, a competitive inhibitor of acetyl-CoA hydrolase, greatly protected the enzyme from inactivation by AsA plus Cu2+, but ATP and ADP, which are both effectors of this enzyme, had only slight protective effects. These results suggest that inactivation of this enzyme by addition of AsA plus Cu2+ was mainly due to attack on its active site.