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At least 19 recordsLinked to original sources
PubMed1976

Mung bean nuclease I. Physical, chemical, and catalytic properties.

A simplified purification procedure for mung bean nuclease has been developed yielding a stable enzyme that is homogeneous in regards to shape and size. The nuclease is a glycoprotein consisting of 29% carbohydrate by weight. It has a molecular weight of 39 000 as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The enzyme contains 1 sulfhydryl group and 3 disulfide bonds per molecule. It has a high content (12.6 mol %) of aromatic residues. Approximately 70% of the enzyme molecules contain a peptide bond cleavage at a single region in the protein. The two polypeptides, 25 000 and 15 000 daltons, are covalently linked by a disulfide bond(s). Both the cleaved and intact forms of the enzyme are equally active in the hydrolysis of the phosphate ester linkages in either DNA, RNA, or adenosine 3'-monophophate. The enzymatic activity of mung bean nuclease can be stabilized at pH 5 in the presence of 0.1 mM zinc acetate, 1.0 mM cysteine, and 0.001% Triton X-100. The enzyme can be inactivated and reactivated by the removal and readdition of Zn2+ or sulfhydryl compounds.

Amino Acids↗
PubMed2026

A Review on Heat Stress in Broiler Chickens: Mechanisms, Effects and Mitigation Strategies.

BACKGROUND: Heat stress (HS) is a major environmental challenge for broilers, particularly under rising global temperatures and high humidity. Broiler chickens are highly susceptible because of their rapid growth rate, high metabolic heat production, limited thermoregulatory capacity and genetic selection for fast growth. OBJECTIVE: This review aims to synthesise current evidence, evaluate the effectiveness of existing mitigation strategies, identify key knowledge gaps and provide future research directions to improve broiler resilience, welfare and productivity under increasingly HS conditions. METHODS: This review synthesised evidence published between 2010 and 2025 on the physiological, metabolic, intestinal, immunological and productive consequences of HS and evaluated mitigation strategies. RESULTS: The reviewed studies demonstrate that HS reduces feed intake by approximately 10%-30%, suppresses body weight gain and feed efficiency and increases mortality, with severity depending on temperature, humidity and broiler genotype. HS disrupts carbohydrate, protein and lipid metabolism; induces acid-base imbalance and oxidative stress; compromises intestinal barrier integrity; alters gut microbiota; suppresses immune function; and reduces meat quality. Nutritional interventions, including dietary electrolyte balance, antioxidants, vitamins, selenium, zinc, phytogenic compounds, probiotics, betaine and optimised feeding strategies, environmental management and genetic approaches, including naked-neck and frizzle genes, can partially alleviate these adverse effects. However, inconsistencies among studies persist because of differences in broiler strains, environmental conditions, dietary formulations and experimental protocols. CONCLUSION: HS substantially compromises broiler health, welfare, productivity and meat quality. Nutritional, environmental and genetic approaches can partially mitigate its adverse effects; however, further research is needed to improve broiler resilience under increasingly HS conditions.

Animals↗
PubMed2024

ZASP: A Highly Compatible and Sensitive ZnCl2 Precipitation-Assisted Sample Preparation Method for Proteomic Analysis.

Universal sample preparation for proteomic analysis that enables unbiased protein manipulation, flexible reagent use, and low protein loss is required to ensure the highest sensitivity of downstream liquid chromatography-mass spectrometry (LC-MS) analysis. To address these needs, we developed a ZnCl2 precipitation-assisted sample preparation method (ZASP) that depletes harsh detergents and impurities in protein solutions prior to trypsin digestion via 10 min of ZnCl2 and methanol-induced protein precipitation at room temperature (RT). ZASP can remove trypsin digestion and LC-MS incompatible detergents such as SDS, Triton X-100, and urea at high concentrations in solution and unbiasedly recover proteins independent of the amount of protein input. We demonstrated the sensitivity and reproducibility of ZASP in an analysis of samples with 1 μg to 1000 μg of proteins. Compared to commonly used sample preparation methods such as SDC-based in-solution digestion, acetone precipitation, FASP, and SP3, ZASP has proven to be an efficient approach. Here, we present ZASP, a practical, robust, and cost-effective proteomic sample preparation method that can be applied to profile different types of samples.

Proteomics↗
PubMed2026

Multitargeted comparative evaluation suggests 2-Aoeobenoxmide shows favourable in silico binding compared to Tucatinib against ERα, HER2, AKT1, EGFR, and PIK3CA in breast cancer.

Breast cancer is a leading cause of cancer-related morbidity and mortality globally, with the WHO reporting approximately 2.3 million new cases and 685,000 deaths annually. Drug resistance in breast cancer complicates treatment, with mutations in critical proteins contributing to therapy failure. Key oncogenic proteins involved in breast cancer progression-namely ERα (a ligand-activated nuclear receptor; PDB: 1A52) and the kinase domains of HER2 (PDB ID: 3PP0), AKT1 (PDB ID: 4EJN), EGFR (PDB ID: 4I23) and PIK3CA (PDB ID: 7R9V)-are pivotal in tumour progression and resistance mechanisms. Targeting these proteins using multitargeted therapeutic strategies may overcome resistance by disrupting key signalling pathways involved in cell proliferation, survival, and metastasis. Such combinatorial approaches promise to improve treatment efficacy and patient outcomes in cases of resistant breast cancer. In this study, we performed multitarget docking on prepared and validated protein structures against the ZINC natural compound library using HTVS, SP, and XP, with pose validation using MM-GBSA. We identified 2-Aoeobenoxmide (2-[1-(2-amino-2-oxo-ethoxy)-6-oxo-benzo[c]chromen-3-yl]oxyacetamide, ZINC134008) with docking and MM-GBSA scores ranging from -8.162 to -10.327 kcal/mol and from -47.18 to -57.62 kcal/mol, respectively, and compared the results with the FDA-approved drug Tucatinib, which exhibited lower binding affinity scores. We further evaluated pharmacokinetic properties using QikProp and electronic properties using DFT (Jaguar) and compared the descriptors of 2-Aoeobenoxmide with those of Tucatinib and with accepted reference ranges. We also performed the WaterMap for 5 nanoseconds (ns), computed various energies, interactions and hydration sites, and the comparison suggests that 2-Aoeobenoxmide shows more favourable hydration-site displacement and binding interactions than Tucatinib. Additionally, a 100 ns MD Simulation has resulted in far less deviation, fluctuations, and intermolecular interactions than Tucatinib, suggesting stable protein-ligand interactions, while the binding free energy and total complex energy computed across 0-1000 frames of the MD trajectories indicate that 2-Aoeobenoxmide is a promising in silico candidate. Importantly, because the entire study is computational, the findings should be interpreted as in silico hypotheses, and experimental validation through in vitro and in vivo assays is warranted before any clinical translation is considered.

Humans↗
PubMed1976

Bovine spleen cathepsin B1 and collagenolytic cathepsin. A comparative study of the properties of the two enzymes in the degradation of native collagen.

Bovine spleen cathepsin B1 and collagenolytic cathepsin were separated by chromatography on Amberlite IRC-50 and collagenolytic cathepsin was partially purified by chromatography on DEAE-Sephadex (A-50). 2. Collagenolytic cathepsin degraded insoluble tendon collagen maximally at pH 3.5 and 28 degrees C; mainly alpha-chain components were released into solution. At 28 degrees C the telopeptides in soluble skin collagen were also cleaved to yield alpha-chain components. Collagenolytic cathepsin was thus similar to cathepsin B1 in its action against native collagen, but mixtures of these two enzymes exhibited a synergistic effect. 3. The addition of thiol-blocking compounds produced similar inhibition of collagenolytic cathepsin and cathepsin B1. The enzyme responded similarly to all other compounds tested except to 6-aminohexanoic acid, when collagenolytic cathepsin was slightly activated and cathepsin B1 was almost unaffected. 4. Leupeptin, which is a structural analogue of arginine-containing synthetic substrates, inhibited collagenolytic cathepsin as effectively as cathepsin B1. Collagenolytic cathepsin was shown to retain a low residual activity against alpha-N-benzoyl-DL-arginine p-nitroanilide during purification which was equivalent to 0.2% of the activity of cathepsin B1. 5. Cathepsin B1 and collagenolytic cathepsin could not be separated by affinity chromatography on organomercurial-Sepharose 4B. The two enzymes could be resolved on DEAE-Sephadex (A-50) and by isoelectric focusing in an Ampholine pH gradient. The pI of the major cathepsin B1 isoenzyme was 4.9 and the pI of collagenolytic cathepsin was 6.4. 6. From chromatography on Sephadex G-75 (superfine grade) the molecular weights were calculated to be 26000 for cathepsin B1 and 20000 for collagenolytic cathepsin. The difference in molecular weight was confirmed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis.

2,2'-Dipyridyl↗
PubMed1975

5"-Amino-3',4',5"-trideoxybutirosin A, a new semisynthetic aminoglycoside antibiotic.

5"-Amino-3',4',5"-trideoxybutirosin A (IX) was synthesized through a reaction series starting from 5"-amino-5"-deoxybutirosin A (Ic), the key step being the treatment of its tetra-O-acetylpentakis-N-((phenylemthoxy)carbonyl)-3',4'-bis-O-(methylsulfonyl) derivative (VI) with zince-sodium iodide. Compound IX inhibits enhanced antibacterial activities, including strains of Pseudomonas aeruginosa and Escherichia coli which are highly resistant to Ic, butirosin or gentamicin.

Anti-Bacterial Agents↗
PubMed1976

The uptake and extrusion of monovalent cations by isolated heart mitochondria.

The factors involved in the movement of monovalent cations across the inner membrane of the isolate heart mitochondrion are reviewed. The evidence suggests that the energy-dependent uptake of K+ and Na+ which results in swelling of the matrix is an electrophoretic response to a negative internal potential. There are no clear cut indications that this electrophoretic cation movement is carrier-mediated and possible modes of entry which do not require a carrier are examined. The evidence also suggests that the monovalent cation for proton exchanger (Na+ greater than K+) present in the membrane may participate in the energy-dependent extrusion of accumulated ions. The two processes, electrophoreti c cation uptake (swelling) and exchange-dependent cation extrusion (contraction) may represent a means of controlling the volume of the mitochondrion within the functioning cell. A number of indications point to the possibility that the volume control process may be mediated by the divalent cations Ca+2 and Mg+2. Studies with mercurial reagents also implicate certain membrane thiol groups in the postulated volume control process.

Animals↗
PubMed1979

The enthalpy of protolysis of liver alcohol dehydrogenase upon binding nicotinamide adenine dinucleotide.

The binding of NAD+, NADH, and ADP-ribose to horse liver alcohol dehydrogenase has been studied calorimetrically as a function of pH at 25 degrees C. The enthalpy of NADH binding is 0 +/- 0.5 kcal mol-1 in the pH range 6 to 8.6. The enthalpy of NAD+ binding, however, varies with pH in a sigmoidal fashion and is -4.0 kcal mol(NAD)-1 at pH 6.0 and +4.5 kcal mol(NAD)-1 at pH 8.6 with an apparent pKa of 7.6 +/- 0.2. The enthalpy of proton ionization of the group on the enzyme is calculated to be in the range 8.8 to 9.8 kcal mol(H+)-1. In conjunction with the available thermodynamic data on the ionization of zinc-bound water in model compounds, it is concluded that the group with a pKa of 9.8 in the free enzyme and 7.6 in the enzyme . NAD+ binary complex is, most likely, the zinc-bound water molecule. Our studies with zinc-free enzyme provide further evidence for this conclusion. Therefore, the processes involving a conformational change of the enzyme upon NAD+ binding and the suggested mechanism of subsequent quenching of the fluorescence of Trp-314 implicating the participation of an ionized tyrosine group must be re-evaluated in the light of this thermodynamic study.

Adenosine Diphosphate Sugars↗
PubMed1975

Localizing -SH groups in monoaminergic synaptic vesicles with the mixture of zinc iodide-osmium tetroxide (ZIO).

In monoaminergic granulated vesicles the mixture of zinc iodide-osmium tetroxide (ZIO) stains two compartments: the core and the matrix, the latter being more intensively stained than the core. Rat pineal glands were incubated in 0.1 M N-ethylmaleimide (NEM). It was observed that NEM blocks ZIO reaction both in the matrix and the core, whereas the controls were fully reactive. This finding strongly suggests that ZIO reaction is due to -SH groups and can be correlated with the effect of NEM on uptake processes.

Animals↗
PubMed1976

Proton equilibria in the binding of Zn2+ and of methylmercuric iodide to papain.

The proton liberation on the binding of zinc chloride and methylmercuric iodide to the (essential) thiol group of papain has been examined as a function of pH. This was carried out by (a) direct titration of the protons on the addition of the metal compound to active papain and (b) measurement of the extent of inhibition of enzyme activity by the metal compound as a function of pH. It was found that in the neutral pH range the thiol group or the neighbouring imidazole group in the free enzyme carries one proton, at low pH both groups do so, whereas at high pH neither group carries a proton. The pK values of the free enzyme that govern the proton release, 4.2 and 8.5, correspond to those that govern overall activity. Both from the experiments with methylmercuric iodide and from fluorescence measurements of methylmercuric papain, it was established that the imidazole group in the latter compound exhibits a pK of 5.4. Taking recent data into account, it was considered that the ion pair of thiolate anion and imidazolium cation, proposed by Polgar, is the best approximation to describe the charge distribution in the active centre and to explain the reaction mechanism.

Binding Sites↗
PubMed1976

Rapid and sensitive colorimetric determination of cobalt(II).

A highly selective and sensitive spectrophotometric determination of cobalt (II) was developed. 7-Nitroso-8-hydroxyquinoline-5-sulfonic acid sodium salt was used as the chromogenic reagent for color development. Although other metals form colored chelates with the ligand, it was possible to develop a selective method using McIlvaine's pH 8 citric acid-phosphate buffer. Under these conditions, iron(II), iron (III), copper (II), zinc (II), and manganese (II), minerals likely to be compounded with cobalt (II) in geriatric formulations, do not interfere with the precision of the method or the color development. Calcium (II) and magnesium (II) do not form colored chelates with the used ligand. Hormones, vitamins, and additives likely to be present along with the cobalt ion in pharmaceutical formulations do not interfere. The sensitivity is 0.37 mug of cobalt (II)/ml of sample solution.

Buffers↗
PubMed1976

Polar-group behaviour in mixed monolayers of phospholipids and fusogenic lipids.

1. The surface potentials of mixed monolayers of synthetic phospholipids with lipids that are fusogenic for hen erythrocytes were investigated. 2. At pH 5.6 and 10, but not at pH2, mixed monolayers of the fusogenic lipid, glycerol mono-oleate, with phosphatidylcholine exhibited negative deviations from the ideality rule in surface potential per molecule which were accompanied by negative deviations in mean molecular area. 3. Interactions of this type were not seen with chemically related but non-fusogenic lipids, nor were they found in mixed monolayers of any of the lipids with phosphatidylethanolamine. 4. Experiments with dihexadecyl phosphate and hexadecyltrimethyl-ammonium indicated that the complete head group of phosphatidylcholine is required for its observed behaviour with fusogenic lipids. 5. Bivalent cations (Ca2+, UO2(2+) or Zn2+) in the subphase at pH 5.6 significantly modified the behaviour of mixed monolayers of fusogenic lipids with phospholipids; there was a parallel perturbing effect of fusogenic lipids on interactions between monolayers of phospholipids and bivalent cations. 6. Possible molecular interactions of fusogenic lipids with membrane phospholipids, and the role of Ca2+, are discussed which may be relevant to cell fusion in erythrocytes induced by low-melting lipids in the presence of Ca2+.

Calcium↗
PubMed1977

Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B.

Human carbonic anhydrase B (HCAB), prepared by a new affinity chromatography procedure, was carboxymethylated exclusively at NT of its active-site histidine-200 using 90% [1-13C]bromoacetate. The 13C nuclear magnetic resonance signal of the covalently attached carboxylate was easily detected over the natural abundance background due to the other carbonyl and carboxyl carbons of this 29 000 molecular weight zinc metalloenzyme. Its chemical shift proved very sensitive to the presence of inhibitors in the active site and to variations in pH. Two perturbing groups with pKa values of 6.0 and 9.2 were assigned to the modified histidine-200 itself and the zinc-bound water ligand, respectively, making use of 13C NMR titration data on Nr- and Nr-carboxymethyl-L-histidine model compounds. The results rule out histidine-200 as the critical group whose ionization controls the catalytic activity. They also strongly suggest an interaction of the carboxylate of the carboxymethyl group with either the zinc or its water ligand around pH 8, possibly explaining the basis for the major differences between HCAB and CmHCAB.

Acetates↗
PubMed1978

Colorimetric determination of arprinocid in feed.

An analytical method has been developed for the determination of arprinocid (9-(2-chloro-6-fluorophenylmethyl)-9H-purin-6-amine) in feed, based upon measurement of the absorbance of the diazo chromophore formed from a product of zinc reduction of the drug in acidic solution. The analyte is extracted from the feed into chloroform in the presence of a pH 7 phosphate buffer and isolated by adsorption chromatography on alumina, followed by partitioning between hexane and 0.15M HCl. The reduction product in the aqueous phase is then treated for colorimetric measurement. This procedure has been applied to determining 0.0010--0.0080% arprinocid in feed with a precision of less than 5% relative standard deviation near the middle of this concentration range. Of 32 feed additives examined, only zoalene and sulfamethazine were serious interferences. A study and discussion of several factors, e.g., reaction time, pH, and amount of zinc metal, that affect the analytical reactions are also included.

Absorption↗
PubMed1976

[Cow's milk alkaline phospharase. II. Subunit structure, metalloproteic nature and kinetic parameters (author's transl)].

Alkaline phosphatase (EC 3.1.3.1) from cow's milk as a dimer comprising two identical or very similar subunits of about 85 000 molecular weight. The enzyme contains 4.9 +/- 0.6 gatoms of zinc per mol of protein. The essential kinetic properties are the same as those of other alkaline phosphatases: variation of pH optimum value, the lack of specificity, increase of Km and V with pH value. The phosphotransferase activity is enlarged, at constant concentration of acceptor, with an increasing concentration of donor. The small size of molecules and the presence of hydroxyls and amino groups increase the percentage of transfer phosphate. The phosphotransferase reaction is better with the D-isomer of serine and the enzyme possesses a more important affinity for the D-phosphoserine.

Alkaline Phosphatase↗
PubMed2026

Identification of compounds that repress DUX4 expression in facioscapulohumeral muscular dystrophy.

Facioscapulohumeral muscular dystrophy (FSHD) is caused by epigenetic dysregulation of the disease locus, leading to pathogenic misexpression of DUX4 in skeletal muscle. Thus, most FSHD therapeutic approaches target DUX4. Our previous study identified the chromatin remodeling factor BAZ1A (bromodomain adjacent to zinc finger domain protein 1A) as a promising target for therapeutic development. Here we used an artificial intelligence-based screening pipeline to identify molecules predicted to bind the BAZ1A bromodomain, and validated hit compounds using FSHD-specific assays in FSHD myocytes. One compound, termed C06, emerged as a potent repressor of DUX4 and DUX4 target gene expression. Interestingly, while C06 exhibited binding to BAZ1A in vitro, it can also inhibit multiple kinases, including p38α, an upstream activator of DUX4. Despite this, at low doses C06 was an equally effective and more specific repressor of DUX4 than losmapimod, which is a robust and specific p38 inhibitor. At low concentrations, C06 returns the DUX4 gene expression signature to a healthier profile without major effects on the muscle transcriptome. Thus, C06 is a useful tool for potent and specific DUX4 suppression, and a viable candidate for further development. Our results highlight both the utility and limitations of AI for targeted drug discovery, and the importance of using an FSHD-specific functional screening strategy for selecting relevant candidates.

Muscular Dystrophy, Facioscapulohumeral↗
PubMed1977

Resonance Raman spectroscopy of arsanilazocarboxypeptidase A: determination of the nature of the azotyrosyl-248-zinc complex.

Resonance Raman spectra of arsanilazotryosyl-248 carboxypeptidase A (peptidyl-L-amino-acid hydrolase, EC 3.4.12.2) exhibit only the vibrational bands of its chromophoric azotyrosyl-248 residue uncomplicated by background interference from either water or other components of the protein. The resonance Raman spectra contain multiple, discrete bands which change as a function of pH, thereby demonstrating the existence of interconvertible species of the azotyrosine probe in solution. Spectra of model azophenols and of the apoazoenzyme establish the identity of these species. All conclusions about the azoenzyme based on the resonance Raman spectra, including the apparent pK values for the interconversion of these species, are in complete agreement with those drawn earlier from studies by absorption spectroscopy. In addition, the properties of resonance Raman bands that have been identified with the motions of specific atoms of azotyrosyl-248 provide details of the interactions of specific atoms of this chromophore with the catalytic zinc atom at the active site. In particular, this has allowed elucidation of the structure of the azotyrosyl-248-zinc coordination complex. Such experiments are also providing information on the effects of crystallization on the enzyme and on its interaction with inhibitors. The important potential of resonance Raman spectroscopy for the study of the structure of chromophoric components of active enzymatic sites and of metal complex ions is discussed.

Arsenicals↗