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EnglishAbstract: Endogenous N-sulfated glycosaminoglycans (GAGs) comigrating with standard heparin and sensitive to nitrous acid treatment were isolated from plasma of healthy donors. The amount of these compounds was 7-10 microg/ml, and activated partial thromboplastin time, anti-Xa and anti-IIa activities were similar to those of standard heparin of high molecular mass. Analysis with gradient PAGE of the putative endogenous heparin showed a mean molecular mass of 12 kD. These N-sulfated GAGs could be isolated only after removal of binding peptides that impaired purification by ion-exchange chromatography. We used SDS-PAGE as a tool to separate peptides from endogenous GAGs. N-sulfated GAGs exited the gel before peptides when the electrophoresis was overrun. Endogenous GAGs could be recovered by ion-exchange chromatography of the SDS-PAGE buffer, 'free' from associating peptides. These results strongly support the hypothesis that endogenous heparin is associated in vitro with a variety of proteins and that this association could be responsible for modification of both heparin and protein activities.
Isolation of endogenous anticoagulant N-sulfated glycosaminoglycans in human plasma from healthy subjects / M. RUGGIERO;M. MELLI;B. PARMA;P. BIANCHINI;S. VANNUCCHI. - In: PATHOPHYSIOLOGY OF HAEMOSTASIS AND THROMBOSIS. - ISSN 1424-8832. - STAMPA. - 32(2002), pp. 44-49.
| Titolo: | Isolation of endogenous anticoagulant N-sulfated glycosaminoglycans in human plasma from healthy subjects | |
| Autori di Ateneo: | ||
| Autori: | RUGGIERO, MARCO; M. MELLI; B. PARMA; P. BIANCHINI; VANNUCCHI, SIMONETTA | |
| Data di pubblicazione: | 2002 | |
| Rivista: | ||
| Volume: | 32 | |
| Pagina iniziale: | 44 | |
| Pagina finale: | 49 | |
| Abstract: | Abstract: Endogenous N-sulfated glycosaminoglycans (GAGs) comigrating with standard heparin and sensitive to nitrous acid treatment were isolated from plasma of healthy donors. The amount of these compounds was 7-10 microg/ml, and activated partial thromboplastin time, anti-Xa and anti-IIa activities were similar to those of standard heparin of high molecular mass. Analysis with gradient PAGE of the putative endogenous heparin showed a mean molecular mass of 12 kD. These N-sulfated GAGs could be isolated only after removal of binding peptides that impaired purification by ion-exchange chromatography. We used SDS-PAGE as a tool to separate peptides from endogenous GAGs. N-sulfated GAGs exited the gel before peptides when the electrophoresis was overrun. Endogenous GAGs could be recovered by ion-exchange chromatography of the SDS-PAGE buffer, 'free' from associating peptides. These results strongly support the hypothesis that endogenous heparin is associated in vitro with a variety of proteins and that this association could be responsible for modification of both heparin and protein activities. | |
| Handle: | http://hdl.handle.net/2158/10102 | |
| Appare nelle tipologie: | 1a - Articolo su rivista |
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