• Journal of the Korean Chemical Society
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• v.18 no.2
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• pp.126-131
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• 1974

Trioctylamine-and tricaprylylmethylammonium chloride-tungstate salts have been prepared by solvent extraction from the sodium tungstate solution of various acidities(pH = 2, 4, 6). The molecular weights of the amine-tungstate salts thus obtained could be cryoscopically measured in benzene by means of a home-built Wheatstone bridge utilizing thermistor with sensitivity of 1/$4000^{\circ}C$. The cryoscopic data along with the results of chemical analysis and infrared spectra of the salts indicate that the amine-tungstates prepared at pH = 2 and 4 are all metatungstate whereas the salt obtained at pH = 6 is an unknown form quite different from the expected paratungstate.R = 0.14. By hydrogen bonding a guanidyl nitrogen of a sulfaguanidine molecule is linked to the sulfonyl oxygens of the other molecules indirectly through two different water molecules. The role of water molecule is both a .
nor and an acceptor in hydrogen-bonding formation and these hydrogen bonds are tetrahedrally o？ented. The hydrogen-bonding networks form infinite molecular layers parallel to (001) plane.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.6-12
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• 1998

To extract insoluble proteins and to improve functional properties of abolished proteins, a protease producing Aspergillus sp. MS-18 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of protease reached to the maximum when the wheat brae medium containing, 3% arabinose, 0.5% polypepton, 0.1% $(NH_4)_2SO_4$ and 0.2% magnesium chloride was cultured for 3 days. Protease was purified 16.9 folds after ion exchange chromatography and gel filtration and the specific activity was 340.4 unit/mg. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of protease was estimated to be 30,000. Crystalization form of purified protease was a stick shape with rounding edges. The optimum pH and temperature for the protease activity were 9.0 and $60^{\circ}C$, respectively. The enzyme was stable in pH 7.0-12.0 at $50^{\circ}C$. The activity of purified enzyme was inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$ and $Pb^{2+}$, whereas it was activited by $Na^+$, $Mg^{2+}$ and $Mn^{2+}$. The activity of the protease was inhibited by the treatment with ethylenediaminetetraacetic acid and phenylmethane sulfonyl fluoride. The result suggests that the purified enzyme is a serine protease with metal ion at active site. Km and Vmax of purified protease were $29.33\;{\mu}mole/L$ and $5.13\;{\mu}g/min$, respectively.