1999
DOI: 10.1023/a:1007776016610
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Cited by 120 publications
(19 citation statements)
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“…The apparent differences between the predicted and observed molecular masses could be accounted for by post-translational modifications as up to four N-glycosylation sites and one O-glycosylation site were predicted (20) by their deduced amino acid sequences. This is consistent with our previous investigation where spiggin assayed positively for the presence of carbohydrate (6). Conversely, only a single distinct protein band of 203 kDa was detected within the urinary bladder of male sticklebacks that also concurred with our previous investigations (6).…”
Section: Discussionsupporting
confidence: 93%
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“…The apparent differences between the predicted and observed molecular masses could be accounted for by post-translational modifications as up to four N-glycosylation sites and one O-glycosylation site were predicted (20) by their deduced amino acid sequences. This is consistent with our previous investigation where spiggin assayed positively for the presence of carbohydrate (6). Conversely, only a single distinct protein band of 203 kDa was detected within the urinary bladder of male sticklebacks that also concurred with our previous investigations (6).…”
Section: Discussionsupporting
confidence: 93%
“…This is consistent with our previous investigation where spiggin assayed positively for the presence of carbohydrate (6). Conversely, only a single distinct protein band of 203 kDa was detected within the urinary bladder of male sticklebacks that also concurred with our previous investigations (6). These observations suggest that formation of spiggin involves multimerization of the constituent kidney subunits in the urinary bladder.…”
Section: Discussionsupporting
confidence: 92%
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