Nicotine and its metabolite, cotinine, in plasma were measured by gas-chromatographic method with flame thermionic detector (FTD-GC) asreported previously. Other variables;e.9.venous blood COHb, total cholesterol, HDL-cholesterol and magnesium in piarma were also measured.Those changes were observed in smoking experiments using habltual or experimental cigarette and abstinence experiment.
ln thirty-five smokers, plasma nicotine and cotinine levels and COHb % were 12.6±1.24ng ml-1,198.9±22.27ng·ml-1 and 5.8±0.41% (x±S.E.), respectiveiy.Plasma nicotine in twenty-two non-smokers was 2.0±0.48ng m1-1, but plasma cotinine was not detectable in almost cases of non-smokers.COHb % in non-smokers was 1.0±0.06%.Total cholesterol, HDL-cholesterol and plasma magnesium in smokers were less than those in non-s mokers.
Although, atherogenic index calculated from total cholesterol and HDL-cholesterol did not show a significant difference between smoker and non-smoker.After one cigarette smoking, plasma nicotine level increased rapidly and reached to maximum immediately or 5 minutes after smoking. At 60 minutes later its level returned to near the level before smoking.Plasma cotinine level elevated more slowly than plasma nicotine.COHb% showed a similar change as plasma nicotine and its change is irrelevant to nicotine yield of cigarette.The decay curve of plasma nicotine after smoking had a slight fluctuation, probabiy due to redistribution and metabolic recycling of nicotine in vivo.
Total cholesterol, HDL-cholesterol, atherogenic index and plasma magnesium had no significant change after smoking.
Plasma nicotine and cotinine levels before or after smoking were variable considerably. lt depends not only daily consumption or nicotine yield of the cigarette smoked but very much on individual moking Pattern.ln this study, the levels of plasmanicotine, cotinine and COHb % correlated slightly with daily consumption and nicotine yield of cigarette.

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simple and rapid methods for the determination of zinc and citric acid in human seminal plasma were examined, using atomic absorption spectrophotometer and isotachophoretic analyzer. Seminal fluid was thoroughly liquefied by standing for 1hr. at room temperature with occasional shaking, follwed by centrifugation (4000rpm). The upper layer (seminal plasma) was diluted 500 times with distilled water and the solution was submitted to atomic absorption spectrophotometer for the measurement of zinc. Citric acid was also measured by isotachophoretic analyzer after 100 times dilution. Those methods were applied to healthy human seminal plasma and the results showed that concentrations of zinc and citric acid were 2.71±0.53mM (n=9) and 37.78±6.07mM (n=9) respectively, and the correlation coefficient (r) between zinc concentration and citric acid was 0.955.

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A practical method for the assay of piasma kallikrein using a fluorogenic substrate (Carbobenzoxy-phenylalanyl-arginine-7-methylcoumarin amide) was described.Prekallikrein was activated with kaolin or dextran sulfate under various conditions at 0°.Treatment of kaolin suspension (6.25mg/ml tris-Hcl buffer, volume ratio to plasma 20: 1) showed highest activation during 20minutes to 40minutes. Optimal conditlons for assay of plasma prekailikrein and plasma spontaneous kallikrein were as follows: substrate concentration 0.1mM and 0.1mM, incubation time 10minutes and 30minutes, plasma volume 100μl and 50μl, respectivility. Heparin used as anticoaguiant affected to plasma kallikrein activity, however sodium citrate and EDTA-2Na did not affected. intra-assay coefficient of variance was 11.2% in plasma spontaneous kalikrein and 3.6% in plasma prekallikrein. A good correation was obtained in values of plasma prekallikrein between chromogenic substrate (H-D-prolyl-phenyialanyl-arginine-P-nitroanilide) method and fluorogenic substrate method. A survey in 26 heaithy sublects showed mean activities of 0.39±0.22nmoie AMC/min/ml at spontaneous kallikrein and 193.4±55.6nmole AMC/min/ml at prekailikrein in plasma, and both values in essential hypertensive patients were not significant by different from those in healthy subject.

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concentration of α₁-microglobulin (α₁-m) in sera and cerebrospinal fluids (CSF) was measured in 121 patients with various neurological disorders. Serum level was determined by single radial immunodiffusion. No significant difference was found between the patients (2.9±0.4mg/dl; Mean±1 S. D.) and normal healthy control group (2.3±0.4mg/dl).The level of α₁-m in CSF was determined using radioimmunoassay of solid antibody system.lts CSF level in the control group was 3.48±1.60μg/dl, while it was significantly increased in the patients with viral meningitis (ρ‹0.01) and cerebral infarct (‹0.05).The level was also elevated in some cases of brain tumor, bacterial meningitis, cerebral hemorrhage, cervical spondylosis, and acute lymphocytic leukemia. There was a positive correlation between α₁-m and albumin levels in CSF. The analysis by CSF/serum albumin and α₁-m ratio suggested that the increase of α₁-m in CSF could be explained mainly by an increase in permeabnity of the serum α₁-m through damaged brain blood barrier under these pathological conditions. lts local production within the central nervous system, however, could not be ruled out in these disorders.

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Three couples of biological guaiacol estrogen isomers (2;3, 5;6, and8;9) and two couples of synthetic ones (11;12, and 14;15) were separated satisfactorily by reversed phase high performance liquid chromatography.
The devised technique involves the elution with a mixture of acetonitrile and water (45: 55) on a column of ODS-SIL monitoring the absorbance at 280nm.
Calibration curves between the amount (μg) of steroid inlected and the peak height (cm) on chrmatogram were linear.The similar linear relationships by internal standard method were obtained for the ratio of guaiacols to estradiol added as an internal standard.
The results for the quantifi Cation of radioactive guaiacols obtained by the incubation of catechol estrogen with rat liver Catechol O-methyltransferase in the presence of [³H-CH₃] - S-adenosyl-L-methionine were in good agreement with the results by other two procedures, reversed isotope dilution and radio thin-layer chromato-scanner methods.

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A kinetic studies on enzymic determinationfor serum cholinesterase activity using cholineoxidase (EC 1.1.3.17) is described.
Preparation of purified enzyme of Cholinesterase is capable to determine serum cholinesterase activity enzymically.
The reacted mechanism of choline oxidase for choline has revealed more complicated steps, because the degradation of choline was proceeded on two ways, lst were liberation step of betain aldehyde., 2nd were formation step of BA´-El complex.
The optimum condition for determination of cholinesterase activity were introduced on the basis of above results.

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There is an upsurge of interest in the serem high-density lipoproteins (HDL), because of their suggested role in atherosclersis and coronary heart diseases.This results in an increased demand for HDL quantitation in the clinical laboratory.To adopt as a routine test, two main questions should have been solved;l) choice of a precipltation method, among others, and 2) methodology of cholestrol determination.
Concerning the first question, we studied several precipitation methods, using the ultracentrifugation method as the reference.Following results were obtained;DS-Mg++method, -2.0%, Pht-Mg++method, +1.7%, Heparin-Ca++method, +3.7%, and Heparin-Mn++ (46mM/l) method, +4.1%.Recovery rates for a-Lipoprotein were (a-lipoprotein content of the original serem was considered as 100%), 93%, 94%, 108%, and 94%, respectively, and HDL contents within the precipitates were 8%, 6%, 0%, and 6% in respective precipitation method.
When enzymatic methods are applied for cholesterol determination, POD-4AA-Phe system was thought to be unsuitable, in terms of sensitivity and interference by the presence of bilirubin and ascorbic acid.In POD-4AA-DMAsystem, however, if determinations were made with absorbance at 550nm, the interference by bilirubin was largely nullified in comparison with the Abell'smethod.Negative interference by ascorbic acid was eliminated by addition of ascorbate oxidase into the system.

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