PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 240516

Simple, sensitive method for measuring plasmin and plasminogen activity in plasma.

T Uete·N Shimano·M Morikawa
View original source ↗Export metadata ↓

Abstract

We describe a sensitive, simple, and rapid method for measuring plasmin and plasminogen in plasma, with fibrinogen as substrate. The assay can be done within 1 h. Plasma is diluted 20-fold with buffer and 0.1 ml (5 mul of original plasma) is incubated for 5 min at 37 degrees C, with or without 400 units of streptokinase. Then 2.0 ml of fibrinogen solution is added, the mixture again incubated (37 degrees C, 5 min), and the reaction stopped. The amount of tyrosine liberated from the fibrinogen is measured and is related to activity. This method is suitable for routine clinical work if the same batch of fibrinogen is used.

Explore related subjects

Enzyme ActivationFemaleFibrinogenFibrinolysinHumansHydrogen-Ion ConcentrationKineticsLiver DiseasesMaleNeoplasmsPlasminogenPregnancyPregnancy Trimester, FirstSpectrophotometryStreptokinaseThrombosisJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T Uete, N Shimano, M Morikawa. 1975. Simple, sensitive method for measuring plasmin and plasminogen activity in plasma.. https://pubmed.ncbi.nlm.nih.gov/240516/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Characterization of raffinose synthase from rice (Oryza sativa L. var. Nipponbare).

The putative raffinose synthase gene from rice was cloned and expressed in Escherichia coli. The enzyme displayed an optimum activity at 45 degrees C and pH 7.0, and a sulfhydryl group was required for its activity. The enzyme was specific for galactinol and p-nitrophenyl-alpha-D-galactoside as galactosyl donors, and sucrose, lactose, 4-beta-galactobiose, N-acetyl-D-lactosamine, trehalose and lacto-N-biose were recognized as galactosyl acceptors.

Enzyme Activation↗
PubMed2007

A comparison of enzymatic phosphorylation and phosphatidylation of beta-L- and beta-D-nucleosides.

Enzymatic 5'-monophosphorylation and 5'-phosphatidylation of a number of beta-L- and beta-D-nucleosides was investigated. The first reaction, catalyzed by nucleoside phosphotransferase (NPT) from Erwinia herbicola, consisted of the transfer of the phosphate residue from p-nitrophenylphosphate (p-NPP) to the 5'-hydroxyl group of nucleoside; the second was the phospholipase D (PLD)-catalyzed transphosphatidylation of L-alpha-lecithin with a series of beta-L- and beta-D-nucleosides as the phosphatidyl acceptor resulted in the formation of the respective phospholipid-nucleoside conjugates. Some beta-L-nucleosides displayed similar or even higher substrate activity compared to the beta-D-enantiomers.

Enzyme Activation↗
PubMed2007

Efficient regeneration of NADPH using an engineered phosphite dehydrogenase.

The in situ regeneration of reduced nicotinamide cofactors (NAD(P)H) is necessary for practical synthesis of many important chemicals. Here, we report the engineering of a highly stable and active mutant phosphite dehydrogenase (12x-A176R PTDH) from Pseudomonas stutzeri and evaluation of its potential as an effective NADPH regeneration system in an enzyme membrane reactor. Two practically important enzymatic reactions including xylose reductase-catalyzed xylitol synthesis and alcohol dehydrogenase-catalyzed (R)-phenylethanol synthesis were used as model systems, and the mutant PTDH was directly compared to the commercially available NADP(+)-specific Pseudomonas sp. 101 formate dehydrogenase (mut Pse-FDH) that is widely used for NADPH regeneration. In both model reactions, the two regeneration enzymes showed similar rates of enzyme activity loss; however, the mutant PTDH showed higher substrate conversion and higher total turnover numbers for NADP(+) than mut Pse-FDH. The space-time yields of the product with the mutant PTDH were also up to fourfold higher than those with mut Pse-FDH. In particular, a space-time yield of 230 g L(-1) d(-1) xylitol was obtained with the mutant PTDH using a charged nanofiltration membrane, representing the highest productivity compared to other existing biological processes for xylitol synthesis based on yeast D-xylose converting strains or similar in vitro enzyme membrane reactor systems.

Enzyme Activation↗