Unstable Flow of Viscoelastic Fluids : 1st Report, Experiment on the Secondary Unstable Flow

紀夫, 進邦; 幸雄, 富田; 静雄, 川瀬

doi:10.1299/kikaib.45.1408

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“…Even the 4-nitroaniline leaving group probably interacts with the enzyme at subsite Si. Previously reported assays of endopeptidase EC 3.4.24.11 usually utilized a hydrophobic Phe residue [6,9,10], but Leu seems preferable in reaching higher kcat values [6]. The Leu residue is also preferable for the present two-stage assay utilizing Streptomyces aminopeptidase, since this enzyme very rapidly hydrolyzes the product of the endopeptidase attack, Leu-NH-Np [ll].…”

Section: Resultsmentioning

confidence: 99%

“…1). This sensitivity exceeds immunoassay levels of detection and may substitute and/or supplement these assays in studies of CALLA, which is nearly identical to human endopeptidase EC 3.4.24.11 [8,9]. Human neutrophils from a healthy donor (5 x 10' cells/ml) hydrolyze the substrate (0.4 mM, pH 7.5) at a fast rate: approx.…”

Section: Resultsmentioning

confidence: 99%

“…the enkephalins, substance P and atria1 natriuretic factor (review [7]). Recently, a near identity in amino acid sequence between human endopeptidase EC 3.4.24.11 and the common acute lymphoblastic leukemia antigen (CALLA, CD 10) has been established [8,9], raising the possibility that it may be involved in yet other functions related to cell differentiation and proliferation.…”

Section: Introductionmentioning

confidence: 99%

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Investigation of neutral endopeptidases (EC 3.4.24.11) and of neutral proteinases (EC 3.4.24.4) using a new sensitive two‐stage enzymatic reaction

et al. 1989

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A sensitive two-stage enzymatic reaction for mammalian and bacterial metalloendopeptidases has been developed using the substrate 3-carboxypropanoyl-alanyl-alanyl-leucine-~nitroanilide supplemented with Streptomyces griseus aminopeptidase. Neutral endopeptidase EC 3.4.24.11 from bovine kidney hydrolyzes the substrate (pH 7.5,25"C) with a catalytic efficiency (k,, = 1.2 x 107 s-r, K,,, = 0.15 mM) of the highest ever reported for the enzyme acting on synthetic chromophoric and fluorogenic substrates. Thermolysin hydrolyzes the substrate at a faster rate (& = 1.2 x 1P s-l) but the overall efficiency is diminished by a higher K,,, (4.2 mM). Suspensions of human neutrophil cells and culture filtrates of BuciNus cereus have been assayed sensitively for their neutral endopeptidase and neutral proteinase activities, respectively. The assay provides a convenient tool for the kinetic investigation of neutral endopeptidases and neutral proteinases and for assessing their function in biological systems.Neutral endopeptidase; Neutral proteinase; Enkephalinase; Thermolysin; Common acute lymphoblastic leukemia antigen

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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