Studies on the reaction of fluorescamine with primary amines

Bernardo, Silvano De; Weigele, Manfred; Toome, V.; Manhart, Karin; Leimgruber, W.; Bőhlen, Peter; Stein, Stanley J.; Udenfriend, Sidney

doi:10.1016/0003-9861(74)90490-1

Cited by 283 publications

(117 citation statements)

References 15 publications

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“…The batch to batch reproducibility of conversion was also within 5% error. Since the chemical yield of the fluorophore is dependent to some extent on the structure of the amine [40] the acquired conversion values can be considered as approximates. The transformation reaction to prepare amino-functional Pluronic was repeated in aqueous medium instead of methanol.…”

Section: Results and Discussion 31 Preparation And Characterization Ofmentioning

confidence: 99%

Preparation and characterization of cationic Pluronic for surface modification and functionalization of polymeric drug delivery nanoparticles

Gyulai

Magyar²,

Rohonczy

et al. 2016

Express Polym. Lett.

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Section: Results and Discussion 31 Preparation And Characterization Ofmentioning

confidence: 99%

Preparation and characterization of cationic Pluronic for surface modification and functionalization of polymeric drug delivery nanoparticles

Gyulai

Magyar²,

Rohonczy

et al. 2016

Express Polym. Lett.

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“…The water-methanol phase was collected and evaporated to dryness, and the primary amines Ser and Etn were subsequently derivatized with fluorescamine exactly as described (26). The deuterated to cold ratio was determined using mass spectrometry.…”

Section: Methodsmentioning

confidence: 99%

The CDP-ethanolamine Pathway and Phosphatidylserine Decarboxylation Generate Different Phosphatidylethanolamine Molecular Species

Bleijerveld

Brouwers

Vaandrager

et al. 2007

Journal of Biological Chemistry

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In mammalian cells, phosphatidylethanolamine (PtdEtn) is mainly synthesized via the CDP-ethanolamine (Kennedy) pathway and by decarboxylation of phosphatidylserine (PtdSer). However, the extent to which these two pathways contribute to overall PtdEtn synthesis both quantitatively and qualitatively is still not clear. To assess their contributions, PtdEtn species synthesized by the two routes were labeled with pathway-specific stable isotope precursors,

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“…Alternatively. an aliquot of the filtrate was subjected to a fluorometric assay using fluorescamine [59] with determination of the amounts of trichloroacetic acid-soluble peptides liberated. 1 U enzyme corresponded to the amount that caused release of about 10 pmol Leu equivalents of trichloroacetic acid-soluble peptidedmin.…”

Section: Assay Of Hemoglobin-digesting Activitymentioning

confidence: 99%

Rabbit procathepsin E and cathepsin E

Kageyama

1993

European Journal of Biochemistry

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The structure of rabbit procathepsin E was determined by molecular cloning of its cDNA. The proenzyme consisted of 379 amino acids and had structural features common to human and guineapig procathepsin E species. The highly conserved tripeptide sequence at the active site of aspartic proteinases, Asp-Thr(Ser)-Gly, is, however, replaced by Asp-Thr-Val in rabbit procathepsin E. To our knowledge, this is the first case of such a variation in aspartic proteinases. The processed form, cathepsin E, hydrolyzed various biologically active peptides maximally at around pH 5. Tachykinins, such as substance P and neurokinin A, were hydrolyzed most rapidly, with specific cleavage of sequences essential for their activity. The rates of hydrolysis were several hundred-fold higher than those of cathepsin D. Furthermore, cathepsin E was able to inactivate a functional-domain peptide of fibroblast growth factor, the sequence of which resembles those of tachykinins, and it was active in the generation of functional peptides, such as endothelin and angiotensin I, from their respective precursors. Procathepsin E was detected at high levels in various fetal tissues, such as the liver, stomach and blood cells. At the adult stage, the proenzyme was detectable only in specific tissues, such as the urinary bladder, duodenum and colon. Northern-blot analysis showed similar stagespecific and tissue-specific expression of the mRNA for procathepsin E. Since tachykinins and other suited peptide substrates of cathepsin E have been shown to have mitogenic activity, (pro)cathepsin E may regulate the growth and differentiation of embryonic and fetal tissues by degrading or processing these peptides. The enzyme may also regulate the physiological activities of adult tissues which are mediated by substance P and related tachykinins.Procathepsin E is known as the precursor of cathepsin E, which is a non-secretory intracellular proteinase [I] Note. The nucleotide sequence reported in this paper has been submitted to the GenBankTMEMBL Data Bank with the accession number L08418.features are not found in other aspartic proteinases and they are correlated with the functional characteristics of procathepsin E, such as stability at alkaline pH [8] and the mechanism of activation of the proenzyme [8, 151. To confirm these unusual structural features, it seems appropriate to elucidate the structures of procathepsin E from different sources.The processed form of the enzyme, cathepsin E, is a typical endoproteinase and digests hemoglobin [5,8,9] and other protein substrates [ l , 8, 9, 161 efficiently. Cathepsin E has been suggested to play an important role in the intracellular processing or degradation of proteins, for example, in the processing of antigen in tissues associated with the immune system [17], in self-destruction of erythrocytes [lo] and the surface epithelial cells of the stomach [7]. However, it remains to be determined whether or not cathepsin E functions under physiological conditions, since the enzyme has been shown to be maximally activ...

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Studies on the reaction of fluorescamine with primary amines

Cited by 283 publications

References 15 publications

Preparation and characterization of cationic Pluronic for surface modification and functionalization of polymeric drug delivery nanoparticles

Preparation and characterization of cationic Pluronic for surface modification and functionalization of polymeric drug delivery nanoparticles

The CDP-ethanolamine Pathway and Phosphatidylserine Decarboxylation Generate Different Phosphatidylethanolamine Molecular Species

Rabbit procathepsin E and cathepsin E

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