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1.
Chinese Journal of Digestion ; (12)2001.
Artículo en Chino | WPRIM | ID: wpr-574597

RESUMEN

Objective To clone human pancreatic cancer gene PTCH,construct the recombinant(expression) plasmid PET22b/PTCH and express the fusion protein.Methods The PTCH gene was(amplified) by RT-PCR from the total RNA extracted from human pancreatic cancer strain SW1990. The amplified product was inserted into the vector PET22b to construct the recombinant expression plasmid PET22b/PTCH,which was transformed into E.coliBL21-CodonPlus~(TM)-RP and then identified by(sequence) analysis.The expression of fusion protein was induced with IPTG and verified by Western blot method.Results A human pancreatic cancer gene with a reading frame of 789 bp was successfully cloned from human pancreatic cancer strain SW1990,which had the same sequence as that of PTCH gene in Genbank.The expression of PET22b/PTCH was proved by Western blot.Conclusion Human(pancreatic) cancer gene PTCH was successfully cloned and constructed with PET22b plasmid.The(prepared) fusion protein lays the basis for further study.

2.
Medical Journal of Chinese People's Liberation Army ; (12)1982.
Artículo en Chino | WPRIM | ID: wpr-551791

RESUMEN

To investigate the distribution of IS605 in Helicobacter pylori(Hp) isolated from Chinese patients, and its relationship to gastroduodenal diseases. The fragment in IS605 was amplified by polymerase chain reaction(PCR) in 107 Hp strains from Chinese patients. Results: The amplicom to IS605 was positive in 47 strains. Detective rates of IS605 in Hp from duodenal ulcer (13.6%) were lower than that from gastritis(52.2%). It suggested that: the detection of IS605 was related to alternation in virulence of Hp.

3.
Academic Journal of Second Military Medical University ; (12)1982.
Artículo en Chino | WPRIM | ID: wpr-551125

RESUMEN

The increased binding of serum a-fetoprotein (AFP) from patients with hepatocellular carcinoma (HCC) to fucose-recognizing lectins has been reported. In order to study the enzymatic basis of this alteration, the serum activities of a-L-fucosidase (AFU) and fucosylated AFP (F-AFP) were determined in serum samples from 90 patients with HCC. Serum F-AFP levels were not related with serum AFU activities in HCC patients. When HCC patients grouped according to AFU activities were analyzed, the mean F-AFP level in 47 patients with a AFU activity below 550 nmol. ml-1. h-1 was 40%?23%, while the corresponding value for 43 patients with a AFU activity above 550 nmol . ml-1. h-1 was 45%?22%. No statistical significance was found between these values. The results indicate that changes in sugar chain structure of AFP in HCC patients do not result from increased or decreased activities of serum AFU.

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