WordNet

send a message from one computer to another to check whether it is reachable and active; "ping your machine in the office"
a sharp high-pitched resonant sound (as of a sonar echo or a bullet striking metal)
contact, usually in order to remind of something; "Ill ping my accountant--April 15 is nearing"
hit with a pinging noise; "The bugs pinged the lamp shade"
make a short high-pitched sound; "the bullet pinged when they struck the car"
street name for lysergic acid diethylamide (同)back breaker, battery-acid, dose, dot, Elvis, loony toons, Lucy in the sky with diamonds, pane, superman, window pane, Zen
any of various water-soluble compounds having a sour taste and capable of turning litmus red and reacting with a base to form a salt
having the characteristics of an acid; "an acid reaction"
the 16th letter of the Roman alphabet (同)p

PrepTutorEJDIC

(小銃弾などの)ピュー(ブーン)という音 / ピュー(ブーン)と音がする
酸性の / 酸味のある,すっぱい(sour) / (言葉・態度などが)厳しい,しんらつな / 酸 / すっぱいもの / 《俗》=LSD
parking
phosphorusの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/08 17:35:14」(JST)

wiki en

4-Chloromercuribenzoic acid (p-chloromercuribenzoic acid, PCMB) is an organomercury compound that is used as a protease inhibitor, especially in molecular biology applications.

PCMB reacts with thiol groups in proteins and is therefore an inhibitor of enzymes that are dependent on thiol reactivity, including cysteine proteases such as papain and acetylcholinesterase. Because of this reactivity with thiols, PCMB is also used in titrimetric quantification of thiol groups in proteins.

References

^ 4-Chloromercuribenzoic acid at Sigma-Aldrich

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 尿酸のバランス uric acid balance
2. 胎児の酸塩基の生理学 fetal acid base physiology
3. 妊娠中の葉酸補充 folic acid supplementation in pregnancy
4. ポルフィリン症：概要 porphyrias an overview
5. 疾患予防におけるビタミン補給 vitamin supplementation in disease prevention

English Journal

Evidence for an Angiotensin-(1-7) Neuropeptidase Expressed in the Brain Medulla and CSF of Sheep.

Marshall AC1, Pirro NT, Rose JC, Diz DI, Chappell MC.Author information 1Hypertension and Vascular Research Center, Wake Forest School of Medicine, Winston Salem, NC.AbstractAngiotensin-(1-7) [Ang-(1-7)] is an alternative product of the brain renin-angiotensin system (RAS) that exhibits central actions to lower blood pressure and improve baroreflex sensitivity. We previously identified a peptidase that metabolizes Ang-(1-7) to the inactive metabolite product Ang-(1-4) in CSF of adult sheep. The current study purified the peptidase 1445-fold from sheep brain medulla and characterized this activity. The peptidase was sensitive to the chelating agents o-phenanthroline and EDTA, as well as the mercury compound p-chloromercuribenzoic acid (PCMB). Selective inhibitors to angiotensin-converting enzyme, neprilysin, neurolysin, and thimet oligopeptidase did not attenuate activity; however, the metallopeptidase agent JMV-390 was a potent inhibitor of Ang-(1-7) hydrolysis (Ki = 0.8 nM). Kinetic studies using 125 I-labeled Ang-(1-7), Ang II, and Ang I revealed comparable apparent Km values (2.6, 2.8 and 4.3 μM, respectively), but a higher apparent Vmax for Ang-(1-7) (72 vs. 30 and 6 nmol/min/mg, respectively; P<0.01). HPLC analysis of the activity confirmed the processing of unlabeled Ang-(1-7) to Ang-(1-4) by the peptidase, but revealed <5% hydrolysis of Ang II or Ang I, and no hydrolysis of neurotensin, bradykinin or apelin-13. The unique characteristics of the purified neuropeptidase may portend a novel pathway to influence actions of Ang-(1-7) within the brain. This article is protected by copyright. All rights reserved.
Journal of neurochemistry.J Neurochem.2014 Mar 25. doi: 10.1111/jnc.12720. [Epub ahead of print]
Angiotensin-(1-7) [Ang-(1-7)] is an alternative product of the brain renin-angiotensin system (RAS) that exhibits central actions to lower blood pressure and improve baroreflex sensitivity. We previously identified a peptidase that metabolizes Ang-(1-7) to the inactive metabolite product Ang-(1-4) i
PMID 24661079

Rapid CO2 permeation across biological membranes: implications for CO2 venting from tissue.

Hulikova A1, Swietach P.Author information 1Department of Physiology, Anatomy, and Genetics, University of Oxford, Oxford, United Kingdom.AbstractThe degree to which cell membranes are barriers to CO2 transport remains controversial. Proteins, such as aquaporins and Rh complex, have been proposed to facilitate CO2 transport, implying that the nonchannel component of membranes must have greatly reduced CO2 permeability. To determine whether membrane CO2 permeation is rate limiting for gas transport, the spread of CO2 across multicellular tissue growths (spheroids) was measured using intracellular pH as a spatial readout. Colorectal HCT116 cells have basal water and NH3 permeability, indicating the functional absence of aquaporins and gas channels. However, CO2 diffusivity in HCT116 spheroids was only 24 ± 4% lower than in pure water, which can be accounted for fully by volume exclusion due to proteins. Diffusivity was unaffected by blockers of aquaporins and Rh complex (Hg2+, p-chloromercuribenzoic acid, and 4,4'-diisothiocyano-2,2'-stilbene-disulfonic acid) but decreased under hypertonic conditions (by addition of 300 mOsm mannitol), which increases intracellular protein crowding. Similar CO2 diffusivity was measured in spheroids of T47D breast cells (basal water permeability) and NHDF-Ad fibroblasts (aquaporin-facilitated water permeability). In contrast, diffusivity of NH3, a smaller but less lipophilic gas, was considerably slower than in pure water, as expected from rate-limiting membrane permeation. In conclusion, membranes, even in the functional absence of proposed gas channels, do not restrict CO2 venting from tissue growths.-Hulikova, A., Swietach, P. Rapid CO2 permeation across biological membranes: implications for CO2 venting from tissue.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology.FASEB J.2014 Mar 20. [Epub ahead of print]
The degree to which cell membranes are barriers to CO2 transport remains controversial. Proteins, such as aquaporins and Rh complex, have been proposed to facilitate CO2 transport, implying that the nonchannel component of membranes must have greatly reduced CO2 permeability. To determine whether me
PMID 24652949

Enhanced activity of an angiotensin-(1-7) neuropeptidase in glucocorticoid-induced fetal programming.

Marshall AC1, Shaltout HA2, Pirro NT1, Rose JC3, Diz DI1, Chappell MC4.Author information 1Hypertension and Vascular Research Center, Wake Forest School of Medicine, Winston Salem, NC, United States.2Hypertension and Vascular Research Center, Wake Forest School of Medicine, Winston Salem, NC, United States; Department of Obstetrics and Gynecology, Wake Forest School of Medicine, Winston Salem, NC, United States; Department of Pharmacology and Toxicology, School of Pharmacy, Alexandria University, Egypt.3Department of Obstetrics and Gynecology, Wake Forest School of Medicine, Winston Salem, NC, United States.4Hypertension and Vascular Research Center, Wake Forest School of Medicine, Winston Salem, NC, United States. Electronic address: mchappel@wakehealth.edu.AbstractWe previously identified angiotensin converting enzyme (ACE) and an endopeptidase activity that degraded angiotensin-(1-7) [Ang-(1-7)] to Ang-(1-5) and Ang-(1-4), respectively, in the cerebrospinal fluid (CSF) of 6-month old male sheep. The present study undertook a more comprehensive analysis of the CSF peptidase that converts Ang-(1-7) to Ang-(1-4) in control and in utero betamethasone-exposed sheep (BMX). Characterization of the Ang-(1-7) peptidase revealed that the thiol agents 4-aminophenylmercuric acetate (APMA) and p-chloromercuribenzoic acid (PCMB), as well as the metallo-chelators o-phenanthroline and EDTA essentially abolished the enzyme activity. Additional inhibitors for serine, aspartyl, and cysteine proteases, as well as selective inhibitors against the endopeptidases neprilysin, neurolysin, prolyl and thimet oligopeptidases did not attenuate enzymatic activity. Competition studies against the peptidase revealed similar IC50s for Ang-(1-7) (5μM) and Ang II (3μM), but lower values for Ala(1)-Ang-(1-7) and Ang-(2-7) of 1.8 and 2.0μM, respectively. In contrast, bradykinin exhibited a 6-fold higher IC50 (32μM) than Ang-(1-7) while neurotensin was a poor competitor. Mean arterial pressure (78±1 vs. 94±2mmHg, N=4-5, P<0.01) and Ang-(1-7) peptidase activity (14.2±1 vs 32±1.5fmol/min/ml CSF, N=5, P<0.01) were higher in the BMX group, and enzyme activity inversely correlated with Ang-(1-7) content in CSF. Lower Ang-(1-7) expression in brain is linked to baroreflex impairment in hypertension and aging, thus, increased activity of an Ang-(1-7) peptidase may contribute to lower CSF Ang-(1-7) levels, elevated blood pressure and impaired reflex function in this model of fetal programming.
Peptides.Peptides.2014 Feb;52:74-81. doi: 10.1016/j.peptides.2013.12.006. Epub 2013 Dec 16.
We previously identified angiotensin converting enzyme (ACE) and an endopeptidase activity that degraded angiotensin-(1-7) [Ang-(1-7)] to Ang-(1-5) and Ang-(1-4), respectively, in the cerebrospinal fluid (CSF) of 6-month old male sheep. The present study undertook a more comprehensive analysis of th
PMID 24355101

Japanese Journal

Purification and Characterization of a Highly Thermostable Chitinase from the Stomach of the Red Scorpionfish Scorpaena scrofa with Bioinsecticidal Activity toward Cowpea Weevil Callosobruchus maculatus (Coleoptera: Bruchidae)

LARIBI-HABCHI Hassiba,DZIRIL Maya,BADIS Abdelmalek,MOUHOUB Samia,MAMERI Nabil
Bioscience, Biotechnology, and Biochemistry 76(9), 1733-1740, 2012
… Among the inhibitors and metals tested, p-chloromercuribenzoic acid, N-ethylmaleimide, Hg2+, and Hg+ completely inhibited enzyme activity. … Chitinase activity towards synthetic substrates in the order of p-NP-(GlcNAc)n (n=2 –4) was p-NP-(GlcNAc)2 > … p-NP-(GlcNAc)4 > … p-NP-(GlcNAc)3. …
NAID 130001862745

Existence of an Iron-Oxidizing Bacterium Acidithiobacillus ferrooxidans Resistant to Organomercurial Compounds(Environmental Biotechnology)

TAKEUCHI FUMIAKI,NEGISHI ATSUNORI,NAKAMURA SOSAKU,KANAO TADAYOSHI,KAMIMURA KAZUO,SUGIO TSUYOSHI
Journal of bioscience and bioengineering 99(6), 586-591, 2005-06-25
… could grow in a ferrous sulfate medium (pH2.5) with 0.1μM p-chloromercuribenzoic acid (PCMB) with a lag time of 2d. …
NAID 110002695705

「p-クロロ水銀安息香酸」

4-Chloromercuribenzoic acid^[1]
Names
	IUPAC name (4-Carboxyphenyl)chloromercury
	Other names p-Chloromercurybenzoic acid; p-Chloromercuribenzoate; 4-Chloromercuribenzoate
Identifiers
CAS Registry Number	59-85-8
Abbreviations	PCMB
ChEBI	CHEBI:28420
ChEMBL	ChEMBL575867
ChemSpider	1667
	InChI InChI=1S/C7H5O2.ClH.Hg/c8-7(9)6-4-2-1-3-5-6;;/h2-5H,(H,8,9);1H;/q;;+1/p-1 ; Key: YFZOUMNUDGGHIW-UHFFFAOYSA-M ; InChI=1/C7H5O2.ClH.Hg/c8-7(9)6-4-2-1-3-5-6;;/h2-5H,(H,8,9);1H;/q;;+1/p-1/rC7H5ClHgO2/c8-9-6-3-1-5(2-4-6)7(10)11/h1-4H,(H,10,11); Key: YFZOUMNUDGGHIW-PSWPUYSSAS ;
Jmol-3D images	Image
PubChem	1730
	SMILES O=C(O)c1ccc([Hg]Cl)cc1 ;
Properties
Chemical formula	C7H5ClHgO2
Molar mass	357.16 g·mol−1
Melting point	287 °C (549 °F; 560 K) (dec.)
Hazards
R-phrases	R26/27/28 R33 R50/53
S-phrases	S13 S28 S36 S45 S60 S61
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
	verify (what is: /?)
	Infobox references