Abstract
Two phosphoglycerate kinase enzymes have been purified from the hyperthermophilic eubacterium Thermotoga maritima. One has been shown to be monomeric with a MW of 41 kDa, whilst the other, in contrast to other phosphoglycerate kinases that have been studied, is seen to be tetrameric by gel filtration, with a subunit MW of 70 kDa by SDS PAGE. The tetrameric PGK is a fusion protein with triose phosphate isomerase and has been crystallised from ammonium sulphate in the presence of the triose sugar substrate 3-phosphoglycerate
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
