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Immunolocalization, properties, and functions of schistosoma putative sphingomyelin phosphodiesterase / Mohammad Mahmoud Farhan Alhalbosiy ; Supervised Rashika Ahmed F. Elridi

By: Contributor(s): Material type: TextTextLanguage: English Publication details: Cairo : Mohammad Mahmoud Farhan Alhalbosiy , 2013Description: 173 P. : charts , photographs ; 25cmOther title:
  • التحديد المناعى لمكان و خصائص و وظائف انزيم السفنجومايلين فوسفوداى استريز لدودة الشستوسوما [Added title page title]
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Dissertation note: Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Zoology Summary: The putative parasite tegument-associated neutral sphingomyrlinase (nSMase) was identified in a recent Schistosoma mansoni genome sequencing and analytical study. Primers based on the published sequence were used to clone and sequence the S. haematobium putative nSMase. It was possible to clone and sequence 836 bp near the 5 end, with 96% identities and 98% positives with S. mansoni nSMase
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Thesis Thesis قاعة الرسائل الجامعية - الدور الاول المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.21.Ph.D.2013.Mo.I (Browse shelf(Opens below)) Not for loan 01010110061552000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.21.Ph.D.2013.Mo.I (Browse shelf(Opens below)) 61552.CD Not for loan 01020110061552000

Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Zoology

The putative parasite tegument-associated neutral sphingomyrlinase (nSMase) was identified in a recent Schistosoma mansoni genome sequencing and analytical study. Primers based on the published sequence were used to clone and sequence the S. haematobium putative nSMase. It was possible to clone and sequence 836 bp near the 5 end, with 96% identities and 98% positives with S. mansoni nSMase

Issued also as CD

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