Demonstration and characterization of hippocampal cholinergic neurostimulating peptide (HCNP) processing enzyme activity in rat hippocampus

1996 ◽  
Vol 21 (3) ◽  
pp. 369-376 ◽  
Author(s):  
Yasushi Otsuka ◽  
Kosei Ojika
Keyword(s):  
Enzyme Activity ◽  
Rat Hippocampus ◽  
Processing Enzyme

scholarly journals In vitro conversion of proapoprotein A-I to apoprotein A-I. Partial characterization of an extracellular enzyme activity.

1983 ◽  
Vol 258 (19) ◽  
pp. 11430-11433 ◽  
Author(s):  
C Edelstein ◽  
J I Gordon ◽  
K Toscas ◽  
H F Sims ◽  
A W Strauss ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Extracellular Enzyme ◽  
Extracellular Enzyme Activity ◽  
Partial Characterization

scholarly journals Partial purification and biochemical characterization of a new highly acidic NYSO laccase from Alcaligenes faecalis

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Soad A. Abdelgalil ◽  
Ahmad R. Attia ◽  
Reyed M. Reyed ◽  
Nadia A. Soliman
Keyword(s):  
Enzyme Activity ◽  
Sodium Dodecyl ◽  
Alcaligenes Faecalis ◽  
Maximum Activity ◽  
Sodium Oxalate ◽  
Partial Purification ◽  
Bromophenol Blue ◽  
Bromocresol Purple ◽  
Laccase Enzyme

Abstract Background Due to the multitude industrial applications of ligninolytic enzymes, their demands are increasing. Partial purification and intensive characterization of contemporary highly acidic laccase enzyme produced by an Egyptian local isolate designated Alcaligenes faecalis NYSO were studied in the present investigation. Results Alcaligenes faecalis NYSO laccase has been partially purified and intensively biochemically characterized. It was noticed that 40–60% ammonium sulfate saturation showed maximum activity. A protein band with an apparent molecular mass of ~ 50 kDa related to NYSO laccase was identified through SDS-PAGE and zymography. The partially purified enzyme exhibited maximum activity at 55 °C and pH suboptimal (2.5–5.0). Remarkable activation for enzyme activity was recognized after 10-min exposure to temperatures (T) 50, 60, and 70 °C; time elongation caused inactivation, where ~ 50% of activity was lost after a 7-h exposure to 60 °C. Some metal ions Cu2+, Zn2+, Co2+, Ni2+, Mn2+, Cd2+, Cr2+, and Mg2+ caused strong stimulation for enzyme activity, but Fe2+ and Hg2+ reduced the activity. One millimolar of chelating agents [ethylenediamine tetraacetic acid (EDTA), sodium citrate, and sodium oxalate] caused strong activation for enzyme activity. Sodium dodecyl sulfate (SDS), cysteine-HCl, dithiothreitol (DTT), β-mercaptoethanol, thioglycolic acid, and sodium azide caused strong inhibition for NYSO laccase activity even at low concentration. One millimolar of urea, imidazole, kojic acid, phenylmethylsulfonyl fluoride (PMSF), H2O2, and Triton X-100 caused activation. The partially purified NYSO laccase had decolorization activity towards different dyes such as congo red, crystal violet, methylene blue, fast green, basic fuchsin, bromophenol blue, malachite green, bromocresol purple eriochrome black T, and Coomassie Brilliant Blue R-250 with various degree of degradation. Also, it had a vast range of substrate specificity including lignin, but with high affinity towards p-anisidine. Conclusion The promising properties of the newly studied laccase enzyme from Alcaligenes faecalis NYSO strain would support several industries such as textile, food, and paper and open the possibility for commercial use in water treatment. It will also open the door to new applications due to its ligninolytic properties in the near future.

Characterization of water soluble pentosans of enzyme supplemented dough and breads/ Caracterización de las pentosanas solubles en agua extraídas de masa y pan conteniendo enzimas comerciales

2000 ◽  
Vol 6 (3) ◽  
pp. 197-205 ◽  
Author(s):  
T. Jimenez ◽  
M.A. Martinez-Anaya
Keyword(s):  
Molecular Weight ◽  
Ferulic Acid ◽  
Synergistic Effects ◽  
Extraction Yield ◽  
Water Soluble ◽  
Sugar Composition ◽  
Enzyme Preparations ◽  
Processing Enzyme ◽  
Enzyme Source

Water soluble pentosans (WSP) from doughs and breads made with different enzyme preparations are characterized according to extraction yield, sugar composition, xylose/arabinose ratio and molecular weight (MW) distribution. Extraction yield was greater for dough than for bread samples, ranging from 0.94 to 1.64%, but bread extracts had a higher purity. Percent of pentoses in purified WSP was greater in pentosanase supplemented samples (28-55%) than in control and amylase containing samples (23-32%). Major sugars were xylose and arabinose, but glucose and mannose also appeared in the extracts. The xylose/arabinose (Xyl/Ara) ratio was 1.3-1.6 and underwent small changes during processing. Enzyme addition caused an increase in Xyl/Ara ratio, attributable to a debranching of arabinoxylans (AX) with higher degree of Ara substitution by arabinofuranosidase. Addition of pentosanases had a significant effect in increasing WSP with MW over 39 000, whereas those of low MW changed only slightly. MW distribution depended on enzyme source, and whereas some enzymes showed activity during fermentation others increased their activity during baking. No synergistic effects were observed in studied variables due to the combination of amylases with pentosanases. Protein in WSP extracts eluted together with ferulic acid suggesting they were linked, but not associated with a determined carbohydrate fraction.

Effect of monensin on the levels of tachykinins and their processing enzyme activity in rat dorsal root ganglia

2002 ◽  
Vol 326 (2) ◽  
pp. 89-92 ◽  
Author(s):  
Toshiyuki Chikuma ◽  
Yuji Inomata ◽  
Ken Tsuchida ◽  
Hiroshi Hojo ◽  
Takeshi Kato
Keyword(s):  
Enzyme Activity ◽  
Dorsal Root Ganglia ◽  
Dorsal Root ◽  
Processing Enzyme

scholarly journals Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura
Keyword(s):  
Enzyme Activity ◽  
Culture Medium ◽  
Gel Filtration ◽  
Partial Purification ◽  
Gastric Mucus ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Optimum Ph ◽  
New Type

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.

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