Lysozyme [EC 3.2.1.17] was purified from human tears, serum, and urine of acute monocytic leukemia patients, renal disease patients, and residents in cadmium-polluted areas of Tsushima Island using an affinity adsorbent containing lysozyme-lysate of Micrococcus lysodeikticus cell walls as the ligand. By means of this procedure, leukemia lysozyme was purified 100- to 200-fold with an activity recovery of 80%. It was crystallized at pH 10. This purified preparation appeared homogeneous in disc electrophoresis and showed a specific activity 2.5-fold higher than that of crystalline lysozyme from hen egg-white. Tear lysozyme was also purified to a nearly homogeneous state while the enzymes from normal serum and urine of a nephrosis patient and of residents in cadmium-polluted area were still disc electrophoretically heterogeneous and showed low specific activity as compared with purified leukemia lysozyme.
Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme. Publishing Authors By Initials
Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Journal of biochemistry
VOLUME: 80
Page Numbers: 703-9
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Oct
YEAR: 1976
Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme. Keywords Mesh Terms:
KEYWORDS: Tears
MESH TERMS: enzymology
Chemical & Substance for Abstract: Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme. Information
Substance Name: Muramidase
Registry Number: EC 3.2.1.17
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Country: JAPAN
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MEDLINETA: J Biochem
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