![]() 4-(N-马来酰亚胺基)二苯甲酮结构式
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常用名 | 4-(N-马来酰亚胺基)二苯甲酮 | 英文名 | 4-(N-Maleimido)benzophenone |
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CAS号 | 92944-71-3 | 分子量 | 277.27400 | |
密度 | 1.33g/cm3 | 沸点 | 472.9ºC at 760mmHg | |
分子式 | C17H11NO3 | 熔点 | 155-157ºC | |
MSDS | 中文版 美版 | 闪点 | 223.7ºC | |
符号 |
![]() GHS07 |
信号词 | Warning |
Subunit interactions in the clathrin-coated vesicle vacuolar (H(+))-ATPase complex.
J. Biol. Chem. 274(41) , 28909-15, (1999) The vacuolar (H(+))-ATPases (or V-ATPases) are structurally related to the F(1)F(0) ATP synthases of mitochondria, chloroplasts and bacteria, being composed of a peripheral (V(1)) and an integral (V(0)) domain. To further investigate the arrangement of subuni... |
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Using a low denaturant model to explore the conformational features of translocation-active SecA.
Biochemistry 51(7) , 1369-79, (2012) The SecA molecular nanomachine in bacteria uses energy from ATP hydrolysis to drive post-translational secretion of preproteins through the SecYEG translocon. Cytosolic SecA exists in a dimeric, "closed" state with relatively low ATPase activity. After bindin... |
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A cross-linking study of the N-terminal extension of human cardiac troponin I.
Biochemistry 42(34) , 10324-32, (2003) Phosphorylation of the unique N-terminal extension of cardiac troponin I (TnI) by PKA modulates Ca(2+) release from the troponin complex. The mechanism by which phosphorylation affects Ca(2+) binding, however, remains unresolved. To investigate this question,... |
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Formation and properties of smooth muscle myosin 20-kDa light chain-skeletal muscle myosin hybrids and photocrosslinking from the maleimidylbenzophenone-labeled light chain to the heavy chain.
Arch. Biochem. Biophys. 288(2) , 584-90, (1991) Experimental conditions which permit the exchange of smooth muscle 20-kDa light chain into skeletal muscle myosin are described. The hybridization does not result in the regulation of actin-activated ATPase activity of the hybrid myosin by smooth light chain ... |
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Identification of the site of photocross-linking formed in the absence of magnesium nucleotide from SH2 (Cys-697) in myosin subfragment 1 labeled with 4'-maleimidylbenzophenone.
J. Biol. Chem. 266(4) , 2272-5, (1991) The site of photocross-linking between Cys-697 (SH2), prelabeled with 4'-[14C]maleimidylbenzophenone, and the 50-kDa segment of myosin S1 on irradiation in the absence of nucleotide has been determined by isolation of the 20-50-kDa adduct and subsequent trypt... |
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The amino-terminal fragment of gelsolin is cross-linked to Cys-374 of actin in the EGTA-resistant actin-gelsolin complex.
FEBS Lett. 301(1) , 99-102, (1992) It has been shown that the EGTA-resistant actin, one of the two actin molecules associated to gelsolin, can be predominantly cross-linked to gelsolin by benzophenone-4-maleimide (BPM), a photoaffinity-labeling reagent, which was conjugated to Cys-374 of actin... |
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Sulphydryl groups in the template-primer-binding domain of murine leukaemia virus reverse transcriptase. Identification and functional analysis of cysteine-90.
Biochem. J. 296 ( Pt 3) , 577-83, (1993) Treatment of murine leukaemia virus reverse transcriptase with benzophenone 4-maleimide inactivates DNA polymerase activity, but has no effect on the RNAase H function. Kinetic measurements indicated that benzophenone 4-maleimide is a competitive inhibitor wi... |
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Interaction of gelsolin with covalently cross-linked actin dimer.
Biochemistry 31(41) , 10061-9, (1992) One of the two actin molecules in the ternary actin-gelsolin complex was selectively cross-linked to gelsolin when benzophenonemaleimide-actin (BPM-actin) was used [Doi, Y., Banba, M., & Vertut-Doi (1991a) Biochemistry 30, 5769-5777]. Here, we examine the int... |
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Crosslinking of N-acetyllactosamine-containing glycoproteins to galectin-1 with an introduced cysteine using a photoactivatable sulfhydryl reagent.
Biochem. Biophys. Res. Commun. 390(3) , 581-4, (2009) Relatively weak interactions between galectins and their potential ligands can hinder identification of physiological lectin ligands using conventional methods such as affinity purification. We have employed a combination of cysteine mutagenesis with chemical... |
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Cross-link formation between mutant galectins of Caenorhabditis elegans with a substituted cysteine residue and asialofetuin via a photoactivatable bifunctional reagent.
Biol. Pharm. Bull. 34(6) , 929-32, (2011) LEC-1 is the first tandem repeat-type galectin isolated from an animal system; this galectin has two carbohydrate recognition domains in a single polypeptide chain. Because its two lectin domains have different sugar-binding profiles, these domains are though... |