The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
SPECTROSCOPIC STUDIES ON PURIFIED ENZYMES. III. Report
On Lipase, Urease and Tyrosinase
RYOJI ITOH
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1936 年 24 巻 2 号 p. 279-286

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1. The ultraviolet absorption spectra of purified ricinuslipase, urease, tyrosinase, casein, eggalbumin and a number of amino acids have been measured.
2. The absorption spectrum of ricinuslipase showed a band with a maximum at 278mμ.
3. Urease showed a band with its maximum at 265mμ at pH 7.
Fig. 6. Absorption eurve of tyrosin tryptophane, phenylalanine, (a) tryptophane. (b) tyrosin. (e) phenylalanine.
4. Tyrosinase showed a band with a maximum at 276mμ, the band shifted towards the longer wavelengths in an alkaline solution and towards the shorter wavelengths in an acid solution without alternation of absorption curve.
5. Casein showed a band with a maximum at 277mμ (pH 9.2), the band shifted towards the longer wavelengths in an alkaline and the shorter wavelengths in an acid solution without alternation of absorption curve.
6. A band with a maximum at 280mμ was found in eggalbumin.
7. Aliphatic amino acids showed no appreciable absorption band.
8. Aromatic amino acids, tyrosin tryptophane and phenyl-alanine have given absorption with a maximum at 275mμ, 280mμ and 262mμ respectively.
The author is greatly indebted to Prof. Dr. K. Iiodama for his kind criticisms and suggestions throughout this research.
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© The Japanese Biochemical Society
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