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methemoglobin (methb  (Millipore)


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    Structured Review

    Millipore methemoglobin (methb
    Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, <t>methemoglobin;</t> HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.
    Methemoglobin (Methb, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/methb/methemoglobin++methb/pmc11208336-67-2-4
    Average 90 stars, based on 1 article reviews
    methemoglobin (methb - by Bioz Stars, 2026-11
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    Images

    1) Product Images from "Porphyromonas endodontalis HmuY differentially participates in heme acquisition compared to the Porphyromonas gingivalis and Tannerella forsythia hemophore-like proteins"

    Article Title: Porphyromonas endodontalis HmuY differentially participates in heme acquisition compared to the Porphyromonas gingivalis and Tannerella forsythia hemophore-like proteins

    Journal: Frontiers in Cellular and Infection Microbiology

    doi: 10.3389/fcimb.2024.1421018

    Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, methemoglobin; HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.
    Figure Legend Snippet: Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, methemoglobin; HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.

    Techniques Used: Comparison, Activity Assay, Produced, Purification, Concentration Assay, Incubation, SDS Page, Staining

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    Article Title: Plasmon-Tuned Silver Colloids for SERRS Analysis of Methemoglobin with Preserved Nativity
    Article Snippet: Optically tuned silver nanoparticles (AgNP's) functionalized with ω-mercaptoalkanoic acids are synthesized and used as a signal amplifier for the surface-enhanced resonance Raman scattering (SERRS) study of heme cofactor in methemoglobin (metHb).. Even though both mercaptopropionic acid (MPA)and mercaptononanoic acid (MNA)-functionalized AgNP's exemplify vastly enhanced SERRS signal of metHb, MNA-AgNP's amplify the SERRS signal amid preservation of the nativity of the heme pocket, unlike MPA-AgNP's.. The electrostatic interaction between MNA-AgNP's and metHb leads to instant signal enhancement with a Raman enhancement factor (EFSERS) of 4.2 × 10 .

    Article Title: Interaction of methemoglobin with GDA/n-C5H11OH/water assemblies.
    Article Snippet: In the present paper, we studied the interaction between n-dodecylammonium α-glutamate (GDA)/n-C5H11OH/H2O assemblies and methemoglobin by UV–vis spectroscopy, X-ray diffraction, electron spin resonance (ESR), rheology, and freeze-fractured transmission electron microscopy (FF-TEM).. It is found that W/O microemulsion forms at a lower n-pentanol content and O/W microemulsion forms at a lower water content with the addition of methemoglobin.. The existence of methemoglobin reduces the hexagonal liquid crystal region, while the lamellar liquid crystal region is little changed in the presence of methemoglobin.

    Article Title: Porphyromonas endodontalis HmuY differentially participates in heme acquisition compared to the Porphyromonas gingivalis and Tannerella forsythia hemophore-like proteins
    Article Snippet: Except for methemoglobin (metHb; Sigma-Aldrich), protein-heme complexes were prepared by mixing protein and heme at a 1:1.2 molar ratio and incubation at room temperature for 1 hour.

    Article Title: Effect of Iron Chelators on Methemoglobin and Thrombin Preconditioning
    Article Snippet: Approximately two-thirds of the culture medium was replaced at 5–6 days in vitro and then twice weekly, using growth medium containing minimal essential medium (MEM), 23 mM glucose, 2 mM glutamine, and 10 % equine serum (Hyclone, Logan, UT, USA).

    Article Title: Real-time chemiluminescent imaging and detection of reactive oxygen species generated in the UVB-exposed human skin equivalent model.
    Article Snippet: The objective of this study is to image and detect reactive oxygen species (ROS) generated in the UVB-exposed three-dimensional human skin equivalent model (HSEM), EpiDerm 200, because the alternative system needs to be urgently established as a replacement for the skin of experimental animals.. Evidence that the ROS generation is enhanced in the skin of live animals after the UVB exposure was already obtained, by using the real-time chemiluminescent (RT-CL) method consisting of a sensitive CL probe (CLA) and an ultralow light imaging apparatus.. In this study, CL emission due to the reaction of CLA with endogenously generated ROS increased significantly in the UVB-treated HSEM compared with that in the intact HSEM, the maximum level being observed at a dose of 27 mJ/cm.

    Article Title: Comparative studies of interactions of hemoglobin with single-chain and with gemini surfactants.
    Article Snippet: Contents lists available at ScienceDirect Journal of Colloid and Interface Science www.elsevier.com/locate/jcis Comparative studies of interactions of hemoglobin with single-chain and with gemini surfactants Yongsheng Wang, Rong Guo ∗, Juqun Xi School of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou, 225002, People’s Republic of China a r t i c l e i n f o a b s t r a c t Article history: Received 26 August 2008 Accepted 3 December 2008 Keywords: Hemoglobin n-Dodecylammonium α-glutamate Gemini Isothermal titration microcalorimetry The interactions of hemoglobin with glutamic acid-based gemini surfactants (L2G2Cn) and with n-dodecylammonium α-glutamate (GDA) have been studied with isothermal titration microcalorimetry, fluorescence spectroscopy, UV–vis spectroscopy, and circular dichroism.. The results indicate that GDA monomer can make the hemoglobin denatured, and that when the concentration of GDA is higher than cmc, heme monomer is released from the hydrophobic cavity of hemoglobin.. On the other hand, L2G2Cn surfactants can also interact with hemoglobin.

    Molecular Weight:

    Article Title: Comparative antioxidant capacities of quercetin and butylated hydroxyanisole in cholesterol-modified erythrocytes damaged by tert-butylhydroperoxide.
    Article Snippet: 0278-6915/$ see front matter 2011 Elsevier Ltd. A doi:10.1016/j.fct.2011.06.014 Abbreviations: BCD, b-cyclodextrin; BHA, butylate terol; DCF, 20 ,70-dichlorofluorescein; DMSO, dimethyl 1,3,5-hexatriene; Hb, hemoglobin; MBCD, methyl-b-c aldehyde; MetHb, methemoglobin; PL, phospholipids ROS, reactive oxygen species; tBHP, tert-butylhydrope acid-reactive substances; TMA-DPH, 1[40-(trimethylam 1,3,5-hexatriene.. ⇑ Corresponding author.. Tel.

    Article Title: Membrane cholesterol contents influence the protective effects of quercetin and rutin in erythrocytes damaged by oxidative stress.
    Article Snippet: Flavonoids are potent scavengers of reactive oxygen species (ROS) that effectively prevent erythrocyte oxidation.. Their antioxidant activities are governed by their structural characteristics and their ability to interact with and penetrate lipid bilayers.. In order to gain a better understanding of the relationship between cholesterol contents and the antioxidant effectiveness of flavonoids against oxidative damage induced by ROS in cells, here we analyzed the integrity and structural stability of cholesterol-modified (enriched or depleted) and control erythrocytes exposed to tert-butyl hydroperoxide in the presence of quercetin or rutin.



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    Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, <t>methemoglobin;</t> HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.
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    Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, <t>methemoglobin;</t> HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.
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    Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, <t>methemoglobin;</t> HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.
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    Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, methemoglobin; HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Porphyromonas endodontalis HmuY differentially participates in heme acquisition compared to the Porphyromonas gingivalis and Tannerella forsythia hemophore-like proteins

    doi: 10.3389/fcimb.2024.1421018

    Figure Lengend Snippet: Comparison of the proteolytic activity of P. endodontalis and P. gingivalis . (A) Total proteolytic activity in whole bacterial cultures (iron- and heme-rich medium; Hm medium) was determined using azocasein as a substrate. The activity is shown as an increase in absorbance at 450 nm (A 450 ) caused by the release of a colored product within 60 minutes by 1 ml of bacterial culture with an optical density at 600 nm of 1. (B) Susceptibility of human hemoproteins and selected HmuY proteins to degradation by proteases produced by P. endodontalis or P. gingivalis . Purified proteins were added to the bacterial cultures (Hm medium) at a final 2 µM concentration, samples were incubated, collected at the indicated time points, and analyzed by SDS-PAGE and CBB G-250 staining. As a control, Hm medium alone was used instead of bacterial cultures. (C) Protein pattern of P. gingivalis or P. endodontalis proteins in iron- and heme-rich culture medium (Hm medium) without adding host hemoproteins or HmuY proteins. metHb, methemoglobin; HSA, serum albumin; Hpx, hemopexin; HmuY Pg , P. gingivalis HmuY; HmuY Pe , P. endodontalis HmuY homolog; HmuY Tf , T. forsythia HmuY homolog; M, protein molecular mass markers. **** P <0.0001.

    Article Snippet: Except for methemoglobin (metHb; Sigma-Aldrich), protein-heme complexes were prepared by mixing protein and heme at a 1:1.2 molar ratio and incubation at room temperature for 1 hour.

    Techniques: Comparison, Activity Assay, Produced, Purification, Concentration Assay, Incubation, SDS Page, Staining