The Separation And Purification Of Heat Shock Protein 70 From Human Lung Adenocarcinoma Cell Lines A549

Lung cancer is one of the most common malignant tumors. The morbidity and mortality of it has a increasing tendency in recent decades.Therefore,searching a practicable treatment plan becomes one of the need badly solving questions at present.Researches in recently years show that heat shock protein 70-associate tumor peptides can initiate tumor specific cell toxicity T lympholeukocyte reaction,so it is possible to product tumor specific anticancer vaccine in the base of HSP70-associate tumor peptides.The HSP70 is the most conservative and primary group in heat shock proteins family.For the biggest content in majority organism and most significant generation after cell stress,HSP70 get attentions and the further research in HSP family.HSP70 can be divided into three domains in the base of the amino acids' primary structures: (1) the adenosine triphosphate domain is in the extrem of amino group;(2) polypoptides conjugation domain is in the extrem of carboxyl group,it is composed of about 15 KD conservative amino acid sequence behind adenosine triphosphate reacting region,and it is the conjugating site with polypoptides or special proteins.It is similar to the conjugating peptides domain of major histocompability complex ,the difference of homology and function is much bigger.(3) A functional domain which can transform function is composed of 10KD unconservative amino acid sequence in the extrem of carboxyl group.conjuncting with adenosine triphosphate or adenosine triphosphate's hydrolization appears that they can regulate the affinity between HSP70 and protein substrates. Polypeptide and unfolding proteins can enhance the activity of adenosine triphosphate enzyme.When the polypeptide conjuncting functional domain is deleted, the function will lose.It indicates that these two function domain are very important to the...