1995
DOI: 10.1016/0304-4165(95)00028-a
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Carbohydrate specificity of theEscherichia coli P-pilus papG protein is mediated by its N-terminal part

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Cited by 19 publications
(21 citation statements)
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“…1A) in gels containing casein showed one strong proteolytic band with apparent molecular mass around 25 kDa and one weaker component with slightly lower mobility. These two bands correspond to unglycosylated and glycosylated SCCE, respectively (9). In addition, a zone of proteolysis, apparently consisting of one stronger band with molecular mass around 30 kDa, and two weaker bands, one with slightly higher mobility and one with slightly lower mobility than the major band, were seen.…”
Section: Resultsmentioning
confidence: 92%
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“…1A) in gels containing casein showed one strong proteolytic band with apparent molecular mass around 25 kDa and one weaker component with slightly lower mobility. These two bands correspond to unglycosylated and glycosylated SCCE, respectively (9). In addition, a zone of proteolysis, apparently consisting of one stronger band with molecular mass around 30 kDa, and two weaker bands, one with slightly higher mobility and one with slightly lower mobility than the major band, were seen.…”
Section: Resultsmentioning
confidence: 92%
“…Previous studies have shown that high expression of SCCE is found in the skin only (9). On the protein level, this enzyme has so far been detected only in squamous eptithelia undergoing cornification (11,22,26,27).…”
Section: Discussionmentioning
confidence: 97%
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