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1.
Adv Exp Med Biol ; 526: 277-83, 2003.
Article in English | MEDLINE | ID: mdl-12908611

ABSTRACT

The purpose of this study was to investigate the dietary taurine intake and serum taurine levels of women on Jeju Island in Korea. Sixty six married women aged 43.5 +/- 7.1 volunteered for this study: 34 from the city area and 32 from two fishing-farming areas. Diet samples were collected from the participants; the samples included three meals (breakfast, lunch and supper), including snacks, drinks and whatever else the participants had eaten for 24 hours. Taurine levels in the diet and serum were determined as the dabsyl derivative by HPLC with a Rf-detector. The intake of taurine ranged from 8.4 to 767.6 mg/day and its mean value was 163.9 +/- 150.2 mg/day (mean +/- SD). There was a significant difference between the two groups: 114.9 +/- 78.7 for the women from the city area and 215.9 +/- 187.9 mg/day for the women from the fishing-farming areas (p<0.001). The taurine intake of the total diet, including all snacks and drinks, was 2300 +/- 584 g/day for the city area and 2342 +/- 528 g/day for the fishing-farming areas. The daily protein intake was 58.8 +/- 16.4 g for the women of the city area and 65.5 +/- 17.1 g for the women of the fishing-farming areas. There was a significant correlation between the intake of fish/shellfish and taurine (p=0.001) while there was no correlation between the intake of protein and taurine (p=0.057). The taurine levels in serum ranged from 68.6 to 261.6 micromol/L and the mean value was 169.7 +/- 41.5 micromol/L. There was no significant difference between the women from the city area and the women from the fishing-farming areas in serum taurine levels. The correlations of serum taurine levels with serum retinol levels (p=0.016) and alpha-tocopherol (p=0.014) levels were significant. These results suggest that taurine intake is dependent on the fish/shellfish intake and that taurine may play an important role in the retention of antioxidative nutrients.


Subject(s)
Taurine/administration & dosage , Taurine/blood , Adult , Diet , Female , Humans , Korea , Middle Aged
2.
Vision Res ; 24(7): 743-50, 1984.
Article in English | MEDLINE | ID: mdl-6331680

ABSTRACT

Stiles' pi 1 and pi 3 mechanisms are thought to reflect adaptation events at two sites in a single pathway, the first site controlled by the short-wavelength cones alone, the second site controlled by opposing signals from these cones vs the other cone classes. We examined this pathway's temporal integration under conditions that yield the full gamut of possible adaptation states at the two sites. Critical duration of the pi 1/pi 3 pathway was always about 200 msec. In addition, we examined the pi 1 and pi 3 mechanisms of dichromatic vision. Our results suggest that protanopic and deuteranopic vision are characterized by a pi 1/pi 3 pathway similar to that in normal color vision.


Subject(s)
Color Perception/physiology , Color Vision Defects/physiopathology , Humans , Time Factors , Visual Pathways/physiopathology
3.
Appl Environ Microbiol ; 39(4): 812-7, 1980 Apr.
Article in English | MEDLINE | ID: mdl-16345546

ABSTRACT

The effects of culture conditions on arylsulfatase production by six strains of the genus Serratia were studied. Synthesis of arylsulfatases in all six strains was repressed in media with inorganic sulfate or methionine as the sole source of sulfur and derepressed by the addition of tyramine. Serratia marcescens IFO 3046 grew most rapidly and produced a high level of arylsulfatase when cultured on mannitol with inorganic sulfate and tyramine. The derepressed synthesis of arylsulfatase in S. marcescens was not subject to strong catabolite repression. The molecular weight of purified arylsulfatase was determined to be between 46,000 and 49,000. Arylsulfatase from S. marcescens differed in K(m) and V(max) values, substrate specificities, fluoride inhibition, and electrophoretic mobility from the enzyme from K. aerogenes, but had the same molecular weight as the latter.

4.
Biochim Biophys Acta ; 485(1): 134-40, 1977 Nov 23.
Article in English | MEDLINE | ID: mdl-334267

ABSTRACT

A simple and convenient method for preparation of a highly purified arylsulfatase (EC 3.1.6.1) from Klebsiella aerogenes has been developed. Specificity of purification was achieved by using affinity chromatography on a tyrosyl-hexamethylenediamino-beta-1,3-glucan or on a solid phase immunoadsorbent. By using affinity chromatography a homogeneous enzyme was obtained with high yield. It is also proposed that the beads of curdlan type polysaccharide consisting of beta-1,3-glucan can be used as a good matrix for affinity chromatography.


Subject(s)
Arylsulfatases/isolation & purification , Klebsiella pneumoniae/enzymology , Sulfatases/isolation & purification , Chromatography, Affinity/methods , Immunosorbents , Polysaccharides, Bacterial , Tyrosine/analogs & derivatives
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