RE:RE:RE:RE:RE:RE:RE:Plasminogen News from Hema-QuebecHi Bepando
Great to get Fred's comments on this!
I've been in the Chromatography field for about 20 years and I can give a bit of background for who's interested.
Plasminogen is part of a Fibrinolytic system of proteins and one of the more concentrated in the plasma at ~ 2uM (200mg/L). It's a large protein of 92kDa with 791 amino acids. It's been separated form other plasmatic proteins for many years now using affinity or size exclusion chromatography. See an article below from 1985.
The name of the game is capacity (how much of it can you separate in a reasonable amount of tme) and resolution/purity (how specific your end product will be). Hema-Quebec is an Agency for the Quebec province who's role is mainly collection and quality control for whaterever blood products going to be used in Quebec's hopitals. To the best of my knowledge they do not have the mandate of producing drugs that will be sold to patients. This was very probably part of a research project. And it probably took weeks to a group of scientists to isolate and purified enough material to get a few drops. There is 10-15 drops in 1 ml of solution.
The pictures I've seen from the Laval PPPS apparatus, it probably starts with more than 100L of plasma with multiple chromatography columns and fractionation a set of very pure proteins in large amount. As PL said in the past, it's the development of 10 to 15 years of work to get to this point.
Hema-Quebec news is only good news for me and no worry, the scientific community is very small, everybody knows everybody through the scientific litterature.
Good luck to all!
J Chromatogr. 1985 Nov 27;348(1):199-204.
Separation of human Glu-plasminogen, Lys-plasminogen and plasmin by high-performance affinity chromatography on Asahipak GS gel coupled with p-aminobenzamidine.
Ito N, Noguchi K, Kazama M, Shimura K, Kasai K.
Abstract
Human Glu-plasminogen, Lys-plasminogen and plasmin were effectively separated by high-performance affinity chromatography. The affinity adsorbent was prepared by using a micro-particulate polyvinyl alcohol gel (Asahipak GS-gel) as the supporting material and p-aminobenzamidine as the specific ligand. All of the active enzyme and proenzymes were adsorbed. Glu-plasminogen was eluted by changing the pH of the eluent and Lys-plasminogen by using an eluent containing 6-amino-hexanoic acid. This affinity adsorbent recognized the difference between these proenzyme species. For the elution of plasmin, addition of urea was necessary. Plasmin may have been adsorbed through a two-site interaction with the adsorbent. All proteins were eluted as sharp peaks and the time required for one cycle was about 1 h. Fluorimetric detection of eluted protein and on-line assay of enzyme activity using a fluorigenic substrate made it possible to analyse microgram amounts of proteins specifically.