scholarly journals The identification of distinctive forms of human α2-macroglobulin by using the numerical relationship between trypsin binding in α- and β-modes

1979 ◽  
Vol 177 (2) ◽  
pp. 501-508 ◽  
Author(s):  
R M Topping ◽  
A H Craven
Keyword(s):  
Bound States ◽  
Proteinase Inhibitors ◽  
Serine Proteinase ◽  
Preceding Paper ◽  
Hydrolytic Activity ◽  
Clinical Value ◽  
Straight Line ◽  
Hydrolytic Activities ◽  
Linear Differential ◽  
Alpha 1 Antitrypsin

Interactions between the serine proteinase trypsin and the protein proteinase inhibitors in human blood were expressed in terms of a coupled set of non-linear differential equations, which has been solved for each of 110 samples of serum obtained from colleagues and from a variety of hospital sources. Optimization of nine unknown theoretical parameters and 21 experimental rate measurements of the hydrolytic activity of trypsin in free and bound states after admixture with various amounts of a given serum was achieved by an iterative procedure using initial estimates of the parameters derived from the “four-straight-line” model described in the preceding paper [Topping & Seilman (1979) Biochem. J. 177, 493–499.] Such a procedure yielded the following information for each sample of serum examined: (a) the concentrations of alpha 1-antitrypsin and alpha 2-macroglobulin; (b) the unequivocal assignment of alpha 2-macroglobulin into one of seven categories on the basis of trypsin binding in two kinetically differentiated modes (alpha and beta); (c) the hydrolytic activities of trypsin (versus Bz-Arg-OEt) when bound to alpha 1-antitrypsin, and to alpha 2-macroglobulin in the alpha- and beta-modes. Molecular interpretations of the binding of trypsin to alpha 2-macroglobulin are discussed and the potential clinical value of recognizing the nature of such binding is reported.

scholarly journals Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Revathi Gurunathan ◽  
Bin Huang ◽  
Vinoth Kumar Ponnusamy ◽  
Jiang-Shiou Hwang ◽  
Hans-Uwe Dahms
Keyword(s):  
Bacillus Cereus ◽  
Hydrothermal Vents ◽  
Extreme Environments ◽  
Serine Proteinase ◽  
Value Added ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Protease Gene ◽  
Hydrolytic Activities ◽  
Promising Source

AbstractMicrobial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus obtained from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °C temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non-anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicates that this enzyme is suitable for the degradation of poultry waste without the loss of nutritionally essential amino acids which otherwise are lost in hydrothermal processing. Therefore, the proteinase is efficient in environmental friendly bioconversion of animal waste into fertilizers or value added products such as secondary animal feedstuffs.

scholarly journals Novel Recombinant keratin Degrading Subtilisin Like Serine Alkaline Protease from Bacillus Cereus Isolated from Marine Hydrothermal Vent Crabs 

2020 ◽  
Author(s):  
Revathi Gurunathan ◽  
Bin Huang ◽  
Vinoth Kumar Ponnusamy ◽  
Jiang-Shiou Hwang ◽  
Hans-Uwe Dahms
Keyword(s):  
Bacillus Cereus ◽  
Hydrothermal Vents ◽  
Extreme Environments ◽  
Serine Proteinase ◽  
Value Added ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Protease Gene ◽  
Hydrolytic Activities ◽  
Promising Source

Abstract Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 ℃) ranges, with maximal hydrolytic activities at pH 10 and at 50 ℃ temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non- anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicate that the protein is suitable for waste management and value-added product synthesis as well as several research applications.

Plasminogen Activator and Plasminogen Activator Inhibitor Associated with Granulomatous Inflammation: A Study with Murine Leprosy

1984 ◽  
Vol 52 (03) ◽  
pp. 243-249 ◽  
Author(s):  
S Izaki ◽  
T Hibino ◽  
Y Isozaki ◽  
P S Hsu ◽  
M Izaki ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Soluble Fraction ◽  
Proteinase Inhibitors ◽  
Granulomatous Inflammation ◽  
Serine Proteinase ◽  
Plasminogen Activator Inhibitor ◽  
Tissue Type ◽  
Weakly Alkaline ◽  
Heat Stable ◽  
Type Plasminogen Activator

SummaryPlasminogen activator that is associated with the development of hypersensitivity granulomas (gPA) was partially purified from a saline soluble fraction of murine lepromas elicited in “resistant” mice, C57BL/6N. The gPA was shown to consist of two subspecies (23,000 and 48,000 in molecular weight) with essentially identical enzymologic properties. The gPA was found to be a relatively heat stable weakly alkaline serine proteinase with trypsin-like characteristics in the specificity for synthetic substrates and proteinase inhibitors. It showed a high affinity for H- D-Ile-Pro-Arg-pNA (Km = 1.4 × 10-4 M) H-D-Val-Leu-Lys- pNA (Km = 5.2 × 10-4 M), and L-pyroGlu-Gly-Arg-pNA (Km = 9.3 × 10-4 M). The gPA did not demonstrate antigenic cross reaction with urokinase-type or tissue-type plasminogen activator.Two distinct enzymatic regulators of the gPA were also demonstrated in the saline soluble fraction of the hypersensitivity granulomas. The gPA and its regulation are assumed to be correlated with macrophage activation in the hypersensitivity granulomas

Mutations affecting the activity of the cyclodextrin glucanotransferase of Paenibacillus pabuli US132: insights into the low hydrolytic activity of cyclodextrin glucanotransferases

Biologia ◽  
2012 ◽  
Vol 67 (4) ◽  
Author(s):  
Sonia Jemli ◽  
Mamdouh Ben-Ali ◽  
Hajer Ben-Hlima ◽  
Bassem Khemakhem ◽  
Samir Bejar
Keyword(s):  
Hydrolytic Activity ◽  
Influential Factor ◽  
Rational Approach ◽  
Cyclodextrin Glucanotransferase ◽  
Hydrolytic Activities ◽  
Maltogenic Amylase ◽  
Structural Barrier ◽  
First Time

AbstractThe cyclodextrin glucanotransferase from Paenibacillus pabuli US132 (US132 CGTase) was engineered using a rational approach in an attempt to provide it with anti-staling properties comparable to those of the commercial maltogenic amylase (Novamyl). The study aimed to concurrently decrease the cyclization activity and increase the hydrolytic activity of US132 CGTase. A five-residue loop (PAGFS) was inserted, alone or with the substitution of essential residues for cyclization (G180, L194 and Y195), mimicking the case of Novamyl. The findings indicate that, unlike the case of the CGTase of Thermoanerobacterium thermosulfurigenes strain EM1 whose initial high hydrolytic activity was exceptional, these mutations completely abolished the cyclization and hydrolytic activities of the US132 CGTase. This suggests that those mutations are not able to convert conventional CGTases, whose hydrolytic activities are very weak, into hydrolases. Accordingly, and for the first time, a structural barrier at subsite −3 was advanced as an influential factor which might explain the low hydrolytic activity of conventional CGTases.

scholarly journals Isolation and amino-acid sequence of two inhibitors of serine proteinases, members of the squash inhibitor family, from Echinocystis lobata seeds.

1996 ◽  
Vol 43 (3) ◽  
pp. 507-513 ◽  
Author(s):  
D Stachowiak ◽  
A Polanowski ◽  
G Bieniarz ◽  
T Wilusz
Keyword(s):  
Amino Acid ◽  
Proteinase Inhibitors ◽  
Sequence Similarity ◽  
Serine Proteinase ◽  
Exchange Chromatography ◽  
Association Constants ◽  
Cathepsin G ◽  
Amino Acid Residues ◽  
Mature Seeds ◽  
Echinocystis Lobata

Two serine proteinase inhibitors (ELTI I and ELTI II) have been isolated from mature seeds of Echinocystis lobata by ammonium sulfate fractionation, methanol precipitation, ion exchange chromatography, affinity chromatography on immobilized anhydrotrypsin and HPLC. ELTI I and ELTI II consist of 33 and 29 amino-acid residues, respectively. The primary structures of these inhibitors are as follows: ELTI I KEEQRVCPRILMRCKRDSDCLAQCTCQQSGFCG ELTI II RVCPRILMRCKRDSDCLAQCTCQQSGFCG The inhibitors show sequence similarity with the squash inhibitor family. ELTI I differs from ELTI II only by the presence of the NH2-terminal tetrapeptide Lys-Glu-Glu-Gln. The association constants (Ka) of ELTI I and ELTI II with bovine-trypsin were determined to be 6.6 x 10(10) M-1, and 3.1 x 10(11) M-1, whereas the association constants of these inhibitors with cathepsin G were 1.2 x 10(7) M-1, and 1.1 x 10(7) M-1, respectively.

scholarly journals Alpha-1 Antitrypsin and Monocytes

2015 ◽  
Vol 25 (2) ◽  
pp. 32-35
Author(s):  
Danielius Serapinas
Keyword(s):  
Experimental Investigation ◽  
Biological Activity ◽  
Proteinase Inhibitor ◽  
Serine Proteases ◽  
Serine Proteinase ◽  
Serine Proteinase Inhibitor ◽  
Short Term ◽  
Dual Effect ◽  
Soluble Cd14 ◽  
Alpha 1 Antitrypsin

Alpha-1 antitrypsin (AAT) is the main circulating serine proteinase inhibitor. A number of studies suggest that AAT can also exhibit biological activity independent of inhibition of serine proteases. The aim of the study was to make experimental investigation of AAT influence on monocytes stimulated by bacterial endotoxyn . AAT affects monocyte responses to LPS by regulating soluble CD14 release. Here we show that a short-term monocyte exposure to AAT leads to an increase of CD14 levels (p0.05). In parallel, a short-term cell exposure to AAT significantly enhances TNFα release. However, AAT was found to have a dual effect on LPS-induced TNFα release. Probably a rapid increase in AAT concentrations during various inflammatory and infectious conditions may enhance the magnitude of monocyte responses to endotoxin and subsequently accelerate resolution of the inflammatory reaction.

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