New biological activity against phospholipase A2 by Turmerin, a protein from Curcuma longa L.

2008 ◽  
Vol 389 (3) ◽  
pp. 299-303 ◽  
Author(s):  
Mukunda Chethankumar ◽  
Leela Srinivas
Keyword(s):  
Biological Activity ◽  
Enzymatic Activity ◽  
Molecular Mass ◽  
Mixed Type ◽  
Curcuma Longa ◽  
Molar Ratio ◽  
Relative Molecular Mass ◽  
Pharmacological Properties ◽  
Naja Naja ◽  
Burk Plot

Abstract Turmerin is a protein from Turmeric (Curcuma longa L.) with a relative molecular mass of 14 kDa. The protein inhibits the enzymatic activity and neutralises the pharmacological properties, such as cytotoxicity, oedema and myotoxicity of multitoxic phospholipase A2 (NV-PLA2) of cobra (Naja naja) venom at a 1:2.5 molar ratio of NV-PLA2:Turmerin. A Lineweaver-Burk plot indicates that Turmerin follows a linear mixed type of inhibition.

Dissociation of enzymatic activity from lethality and pharmacological properties by carbamylation of lysines in Naja nigricollis and Naja naja atra snake venom phospholipases A2

Toxicon ◽  
1981 ◽  
Vol 19 (5) ◽  
pp. 705-720 ◽  
Author(s):  
Eleonora Condrea ◽  
Jeffrey E. Fletcher ◽  
Bruce E. Rapuano ◽  
Chen-Chung Yang ◽  
Philip Rosenberg
Keyword(s):  
Enzymatic Activity ◽  
Snake Venom ◽  
Pharmacological Properties ◽  
Naja Naja ◽  
Phospholipases A2 ◽  
Naja Atra

Extraction of polyethylene glycols with dicarbolide solutions in nitrobenzene

1990 ◽  
Vol 55 (8) ◽  
pp. 1959-1967 ◽  
Author(s):  
Petr Vaňura ◽  
Pavel Selucký
Keyword(s):  
Polyethylene Glycol ◽  
Molecular Mass ◽  
Extraction Constant ◽  
Metal Extraction ◽  
Polyethylene Glycols ◽  
Relative Molecular Mass ◽  
Published Data ◽  
Average Molecular Mass ◽  
Peg 400 ◽  
Extraction Constants

The extraction of polyethylene glycol of average molecular mass 400 (PEG 400) with dicarbolide solution in nitrobenzene and of longer-chain polyethylene glycol, of average molecular mass 1 500 (PEG 1 500), with chlorinated dicarbolide solution in nitrobenzene was studied. During the extraction of PEG 400, the polyethylene glycol solvates the Horg+ ion in the organic phase giving rise to the HLorg+ species (L is polyethylene glycol). The obtained value of the extraction constant Kex(HLorg+) = 933 is consistent with published data of metal extraction. Extraction of PEG 1 500 was treated applying the simplified assumption that the thermodynamic behaviour of PEG 1 500 is the same as that of n molecules of polyethylene glycol with relative molecular mass 1 500/n, each solvating one cation. For this model, the value of n = 3.2 ± 1.1 and the values of the extraction constants of the HL1/n,org+ and HL2/n,org+ species were obtained by using the adapted program LETAGROP. This value of n is consistent with published extraction data in the presence of polyethylene glycol with a relative molecular mass from 200 to 1 000.

scholarly journals Hydrazones of 4-(Trifluoromethyl)benzohydrazide as New Inhibitors of Acetyl- and Butyrylcholinesterase

Molecules ◽  
2021 ◽  
Vol 26 (4) ◽  
pp. 989
Author(s):  
Martin Krátký ◽  
Katarína Svrčková ◽  
Quynh Anh Vu ◽  
Šárka Štěpánková ◽  
Jarmila Vinšová
Keyword(s):  
Biological Activity ◽  
Mixed Type ◽  
Cholinesterase Inhibitors ◽  
Eukaryotic Cell ◽  
Structure Activity ◽  
Aliphatic Ketones ◽  
Ic50 Values ◽  
Central Nervous Systems ◽  
Dual Inhibition ◽  
Potential Inhibitors

Based on the broad spectrum of biological activity of hydrazide–hydrazones, trifluoromethyl compounds, and clinical usage of cholinesterase inhibitors, we investigated hydrazones obtained from 4-(trifluoromethyl)benzohydrazide and various benzaldehydes or aliphatic ketones as potential inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). They were evaluated using Ellman’s spectrophotometric method. The hydrazide–hydrazones produced a dual inhibition of both cholinesterase enzymes with IC50 values of 46.8–137.7 µM and 19.1–881.1 µM for AChE and BuChE, respectively. The majority of the compounds were stronger inhibitors of AChE; four of them (2-bromobenzaldehyde, 3-(trifluoromethyl)benzaldehyde, cyclohexanone, and camphor-based 2o, 2p, 3c, and 3d, respectively) produced a balanced inhibition of the enzymes and only 2-chloro/trifluoromethyl benzylidene derivatives 2d and 2q were found to be more potent inhibitors of BuChE. 4-(Trifluoromethyl)-N’-[4-(trifluoromethyl)benzylidene]benzohydrazide 2l produced the strongest inhibition of AChE via mixed-type inhibition determined experimentally. Structure–activity relationships were identified. The compounds fit physicochemical space for targeting central nervous systems with no apparent cytotoxicity for eukaryotic cell line together. The study provides new insights into this CF3-hydrazide–hydrazone scaffold.

scholarly journals Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach

Toxins ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 453
Author(s):  
Sebastian Estrada-Gómez ◽  
Leidy Johana Vargas-Muñoz ◽  
Cesar Segura Latorre ◽  
Monica Maria Saldarriaga-Cordoba ◽  
Claudia Marcela Arenas-Gómez
Keyword(s):  
Enzymatic Activity ◽  
Molecular Mass ◽  
Evolutionary Relationship ◽  
Venom Gland ◽  
Duplication Event ◽  
High Molecular Mass ◽  
Amino Acid Sequences ◽  
Secretory Proteins ◽  
Phospholipases A2 ◽  
Kunitz Type

Nowadays, spider venom research focuses on the neurotoxic activity of small peptides. In this study, we investigated high-molecular-mass compounds that have either enzymatic activity or housekeeping functions present in either the venom gland or venom of Pamphobeteus verdolaga. We used proteomic and transcriptomic-assisted approaches to recognize the proteins sequences related to high-molecular-mass compounds present in either venom gland or venom. We report the amino acid sequences (partial or complete) of 45 high-molecular-mass compounds detected by transcriptomics showing similarity to other proteins with either enzymatic activity (i.e., phospholipases A2, kunitz-type, hyaluronidases, and sphingomyelinase D) or housekeeping functions involved in the signaling process, glucanotransferase function, and beta-N-acetylglucosaminidase activity. MS/MS analysis showed fragments exhibiting a resemblance similarity with different sequences detected by transcriptomics corresponding to sphingomyelinase D, hyaluronidase, lycotoxins, cysteine-rich secretory proteins, and kunitz-type serine protease inhibitors, among others. Additionally, we report a probably new protein sequence corresponding to the lycotoxin family detected by transcriptomics. The phylogeny analysis suggested that P. verdolaga includes a basal protein that underwent a duplication event that gave origin to the lycotoxin proteins reported for Lycosa sp. This approach allows proposing an evolutionary relationship of high-molecular-mass proteins among P. verdolaga and other spider species.

scholarly journals Isolation, Structure Elucidation, and Biological Activity of a New Alkaloid from Zanthoxylum rhetsa

2011 ◽  
Vol 6 (11) ◽  
pp. 1934578X1100601
Author(s):  
Karsten Krohn ◽  
Stephan Cludius-Brandt ◽  
Barbara Schulz ◽  
Mambatta Sreelekha ◽  
Pottachola Mohamed Shafi
Keyword(s):  
Biological Activity ◽  
Carboxylic Acid ◽  
Medicinal Plant ◽  
Plant Extract ◽  
Structure Elucidation ◽  
Biologically Active ◽  
Reduction Product ◽  
Pharmacological Properties ◽  
Evergreen Tree

Several biologically active alkaloids (1-4, 6), including a new quinazoline-6-carboxylic acid (1), were isolated from the medicinal plant Zanthoxylum rhetsa, an evergreen tree, native to subtropical areas. Whereas the pharmacological properties of the plant extract and single constituents have been widely tested, we now show that all of the metabolites have antialgal activities, all but 6 are antibacterial, and 6 and the reduction product 5 (derived from 4) are also antifungal.

Towards a molecular description of cell transformation by avian sarcoma virus

1980 ◽  
Vol 210 (1180) ◽  
pp. 387-396 ◽  
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Molecular Mass ◽  
Cellular Protein ◽  
Transformed Cells ◽  
Relative Molecular Mass ◽  
Protein Kinase Activity ◽  
Avian Sarcoma Virus ◽  
Sarcoma Virus ◽  
Avian Sarcoma

The avian sarcoma virus transforming gene product has been identified and partially purified from extracts of transformed cells. It is a phosphoprotein with a relative molecular mass of 60 000 (pp60 src ) with two major sites of phosphorylation. pp60 src appears to be a cyclic-AMP-independent protein kinase as judged by protein phosphorylation with partly purified fractions. The specificity of the phosphorylation observed was judged by inhibition with anti-pp60 src IgG but not by normal IgG and by the fact that the protein kinase activity isolated from ts transformation-mutant infected cells was more thermolabile than that from wild-type transformed cells, thus showing more directly the origin of the enzymic activity. A cellular protein substrate of pp60 src has been identified as a 34000 molecular mass protein. These data together suggest that protein phosphorylation by pp60 src may be a function of the molecule that plays a major role in transformation.

Enzymatic deglycosylation of porcine thyroid peroxidase: effects on catalytic activity and immunoreactivity

1991 ◽  
Vol 124 (1) ◽  
pp. 107-114 ◽  
Author(s):  
Egberto G. Moura ◽  
Carmen C. Pazos-Moura ◽  
Naokata Yokoyama ◽  
Martha L. Dorris ◽  
Alvin Taurog
Keyword(s):  
Catalytic Activity ◽  
Molecular Mass ◽  
Antigenic Determinants ◽  
Enzyme Linked Immunosorbent Assay ◽  
Minor Role ◽  
Relative Molecular Mass ◽  
Thyroid Peroxidase ◽  
Autoimmune Thyroid ◽  
Tryptic Fragment ◽  
A Minor

Abstract Thyroid peroxidase is a heme-containing, membrane-bound, glycoprotein enzyme that catalyzes iodination and coupling in the thyroid gland. It is also the antigen for microsomal autoantibodies that are commonly found in the serum of patients with autoimmune thyroid disease. We examined the effect of deglycosylation on the catalytic functions and the immunoreactivity of this enzyme. A highly purified, solubilized, large tryptic fragment of porcine thyroid peroxidase, retaining all of the N-linked glycosylation sites of the native enzyme and displaying full catalytic activity was used. It was deglycosylated by treatment with N-glycanase under nondenaturing conditions. The loss in relative molecular mass after treatment, determined by gel electrophoresis, was about 75% of the estimated molecular weight of the glycan portion of porcine thyroid peroxidase. Lectin blots performed with horseradish peroxidase-conjugated concanavalin A showed a similar loss in relative molecular mass but some residual carbohydrate. The intensity of the carbohydrate stain was consistent with the loss of about 75% of the glycans. Despite this loss, three different assays for catalytic activity of porcine thyroid peroxidase were not significantly decreased. Immunoreactivity measured by immunoblotting and by enzyme-linked immunosorbent assay was also unimpaired. These findings suggest that N-glycanase-sensitive glycans in porcine thyroid peroxidase do not act as antigenic determinants and play a minor role, if any, in catalytic activity and, presumably therefore, in the maintenance of protein conformation.

Receptors for epidermal growth factor and insulin-like growth factor-I on preimplantation trophoderm of the pig

Development ◽  
1990 ◽  
Vol 110 (1) ◽  
pp. 221-227
Author(s):  
A.N. Corps ◽  
D.R. Brigstock ◽  
C.J. Littlewood ◽  
K.D. Brown
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Molecular Mass ◽  
Cross Linking ◽  
Relative Molecular Mass ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Epidermal Growth ◽  
Growth Factor I

125I-labelled epidermal growth factor (125I-EGF) and 125I-labelled insulin-like growth factor-I (125I-IGF-I) bound to trophoderm cells from pig blastocysts obtained on days 15–19 of pregnancy. Specific binding was detected on freshly isolated cell suspensions and on cells cultured for several days. The binding of 125I-EGF was inhibited by increasing concentrations of EGF, but not by various other growth factors and hormones. Chemical cross-linking of 125I-EGF to its receptors using disuccinimidyl suberate (DSS) revealed a radiolabelled band of relative molecular mass 160,000, similar to that identified as the EGF receptor in other cell types. The binding of 125I-IGF-I was inhibited by both IGF-I and insulin, indicating that the receptors were either type I IGF receptors or insulin receptors. Cross-linking of 125I-IGF-I to serum-free supernatants from trophoderm cultures showed that the cells secreted an IGF-binding protein, giving a complex of relative molecular mass about 45,000. The presence of receptors for EGF and IGF/insulin suggests that these factors could be involved in regulating the growth and development of the early blastocyst.

scholarly journals Physical and kinetic characterization of recombinant human cholesteryl ester transfer protein

1996 ◽  
Vol 320 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Daniel T CONNOLLY ◽  
Jonathan McINTYRE ◽  
Deborah HEUVELMAN ◽  
Edward E REMSEN ◽  
Russell E McKINNIE ◽  
...  
Keyword(s):  
Cholesteryl Ester ◽  
Molecular Mass ◽  
Cholesteryl Ester Transfer Protein ◽  
Mammalian Cells ◽  
Random Coil ◽  
Sedimentation Equilibrium ◽  
Relative Molecular Mass ◽  
Transfer Protein ◽  
Ldl Particles ◽  
Carrier Mechanism

Cholesteryl ester transfer protein (CETP) mediates the exchange of triglycerides (TGs), cholesteryl esters (CEs) and phospholipids (PLs) between lipoproteins in the plasma. In order to better understand the lipid transfer process, we have used recombinant human CETP expressed in cultured mammalian cells, purified to homogeneity by immunoaffinity chromatography. Purified recombinant CETP had a weight-average relative molecular mass (Mw) of 69561, determined by sedimentation equilibrium, and a specific absorption coefficient of 0.83 litre·g-1· cm-1. The corresponding hydrodynamic diameter (Dh) of the protein, determined by dynamic light scattering, was 14 nm, which is nearly twice the expected value for a spheroidal protein of this molecular mass. These data suggest that CETP has a non-spheroidal shape in solution. The secondary structure of CETP was estimated by CD to contain 32% α-helix, 35% β-sheet, 17% turn and 16% random coil. Like the natural protein from plasma, the recombinant protein consisted of several glycoforms that could be only partially deglycosylated using N-glycosidase F. Organic extraction of CETP followed by TLC showed that CE, unesterified cholesterol (UC), PL, TG and fatty acids (FA) were associated with the pure protein. Quantitative analyses verified that each mol of CETP contained 1.0 mol of cholesterol, 0.5 mol of TG and 1.3 mol of PL. CETP mediated the transfer of CE, TG, PL, and UC between lipoproteins, or between protein-free liposomes. In dual-label transfer experiments, the transfer rates for CE or TG from HDL to LDL were found to be proportional to the initial concentrations of the respective ligands in the donor HDL particles. Kinetic analysis of CE transfer was consistent with a carrier mechanism, having a Km of 700 nM for LDL particles and of 2000 nM for HDL particles, and a kcat of 2 s-1. The Km values were thus in the low range of the normal physiological concentration for each substrate. The carrier mechanism was verified independently for CE, TG, PL and UC in ‘half-reaction’ experiments.

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