نتایج جستجو برای: fok1 polymorphism pcr rflp

تعداد نتایج: 269676  

Journal: :Respiratory Research 2005
Geraint B Rogers Mary P Carroll David J Serisier Peter M Hockey Valia Kehagia Graeme R Jones Kenneth D Bruce

BACKGROUND Chronic lung infections are the primary cause of morbidity and mortality in Cystic Fibrosis (CF) patients. Recent molecular biological based studies have identified a surprisingly wide range of hitherto unreported bacterial species in the lungs of CF patients. The aim of this study was to determine whether the species present were active and, as such, worthy of further investigation ...

Molecular typing of twenty-five Pasteurella multocida isolates has been assessed by restriction fragmentlength polymorphism (RFLP) of a species-specific PCR assay. Amplification was based on the gene ompH, encoding a major outer memberane protein. RFLP analysis of the 1.2 kb ompH-amplification usingEcoRI, HindIII and CfoI endonucleases produced 7 different patterns for the twenty fi...

Journal: :FEMS microbiology ecology 2003
Malin Bomberg German Jurgens Aimo Saano Robin Sen Sari Timonen

Archaea colonising defined compartments of Scots pine Suillus bovinus or Paxillus involutus mycorrhizospheres developed in forest humus-containing microcosms were investigated by nested polymerase chain reaction (PCR), cloning, restriction fragment length polymorphism (RFLP) and sequencing. Archaea representing six RFLP groups were detected in the system. Sequence analysis of clones representin...

Journal: :Annals of clinical and laboratory science 1991
S Narayanan

The availability of a variety of restriction endonuclease enzymes that cleave deoxyribonucleic acid (DNA) at specific sites has made it possible to identify the presence of polymorphic regions in the isolated fragments. Such restriction fragment length polymorphism (RFLP) results owing to a variation in the number of tandem repeats (VNTR) of a short DNA segment. These VNTR sequences can uniquel...

Journal: :Clinical chemistry and laboratory medicine 2004
Amir H Shemirani László Muszbek

The Val34Leu polymorphism in the A subunit of blood coagulation factor XIII (FXIII-A) is located in the activation peptide, just three amino acids upstream of the thrombin cleavage site. The Val-->Leu replacement accelerates the rate of the proteolytic activation of FXIII and it seems to provide protection against myocardial infarction. Methods available for the assessment of the FXIII-A Val34L...

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