1980
DOI: 10.1016/0005-2744(80)90510-0
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Chemical modifications of achromobacter collagenase and their influence of the enzymic activity

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1983
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Cited by 5 publications
(2 citation statements)
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“…Previous studies have shown that the subunit of Achromobacter collagenase (strain 1.029) may be structurally similar to the neutral proteinases recovered from Bacillus thermoproteolyticus (thermolysin; EC 3.4.24.4) and B. subtilis (10). This association is based on a comparison of molecular weights, amino acid compositions (9,14,32), essential components of the enzyme active sites (7,33), and circular dichroism measurements (6). However, a comparison of the amino acid compositions of the purified subunits of strain CIP 82.01 and 1.029 collagenases with the amino acid compositions of thermolysin and B .…”
Section: Discussionmentioning
confidence: 99%
“…Previous studies have shown that the subunit of Achromobacter collagenase (strain 1.029) may be structurally similar to the neutral proteinases recovered from Bacillus thermoproteolyticus (thermolysin; EC 3.4.24.4) and B. subtilis (10). This association is based on a comparison of molecular weights, amino acid compositions (9,14,32), essential components of the enzyme active sites (7,33), and circular dichroism measurements (6). However, a comparison of the amino acid compositions of the purified subunits of strain CIP 82.01 and 1.029 collagenases with the amino acid compositions of thermolysin and B .…”
Section: Discussionmentioning
confidence: 99%
“…Comparison of amino acid composition In a previous study, Trocheris et al [28] reported the amino acid composition of V. alginolyticus collagenase from a chemically purified protein sample. The comparison of the two amino acid compositions is shown in Table 3.…”
Section: Elisa With Anti-peptide Antibodiesmentioning
confidence: 99%