Incorporation of small unilamellar liposomes loaded with horseradish peroxidase into isolated nerve endings from electric organ ofTorpedo marmorata
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Horseradish peroxidase
Electric organ
Free nerve ending
Sephadex
Pure cholinergic nerve endings (synaptosomes) were isolated from the electric organ of Torpedo by a rapid procedure. These synaptosomes are approximately 3 micron in diameter. They contain an occasional mitochondrion, numerous synaptic vesicles, and sometimes an active zone is observed. No postynaptic membrane attachment is found. This nerve ending fraction is extremely pure as shown by morphological controls and biochemical data. It is rich in choline acetyltransferase (450 nmol/h per mg protein) and acetylcholine (ACh) (130 nmol/mg protein). The isolated endings retain their cytoplasmic components and they synthesize ACh and are stable in vitro for several hours, as shown by biochemical measurements and morphological analysis.
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The horseradish peroxidase (HRP) potential in organic synthesis.
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The objective of the present work was to examine biocatalytic properties of peroxidase in horseradish acclimatized in our country. We have found that horseradish root extract’s peroxidase (HRP) has Km 2.5 mM and Vmax 5.36 mM·s-1. Maximum activity (pHopt) was estimated at pH 6.0 and enzyme is more stable in alkali, than in acid. The optimum temperature (Topt) for HRP is 40oC and the enzyme is not stable to temperature influence. The horseradish root’s extract retains enzymatic activity within 21 days. DOI: http://doi.dx.org/10.5564/mjc.v15i0.332 Mongolian Journal of Chemistry 15 (41), 2014, p101-103
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The present study describes an easy and efficient procedure for the purification of horseradish peroxidase from horseradish roots. For this purpose, supermacroporous cryogels having Concanavalin A were prepared by photosensitive cross-linking polymerization. Horseradish peroxidase binding and elution from the prepared cryogels were carried out changing various parameters such as initial peroxidase concentration and pH. The best binding performance was obtained at pH 7.0. The maximum horseradish peroxidase binding of the cryogels was found to be 3.85 mg g −1 cryogel. Horseradish peroxidase purification from crude extract resulted in 115.1-fold. SDS-PAGE analysis and circular dichroism measurements indicated that the horseradish peroxidase purification from horseradish roots was successfully carried out.
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Horseradish peroxidase(HRP) is a peroxidase with heme-containing enzyme for redox-center, which isolated from horseradish roots. In recent years, HRP could be applied for wastewater treatment and food industry, organic synthesis as well as chemiluminescent assays. The structure, immobilization and application of horseradish peroxidase were introduced significantly. The present problems and the future advance in the industry of HRP were reviewed.
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セメント細胞と骨細胞の物質輸送経路の相違を観察するため, ラットにトレーサーとしてmicroperoxidase (MP) あるいはhorseradish peroxidase (HRP) を静注した。有細胞セメント質において, HRPはすべてのセメント小腔にみられたが, MPはすべてにはみられなかった。MPまたはHRPは, ほぼすべてのセメント細胞に取り込まれ, ライソゾーム系細胞内小器官に認められた。MPは成熟セメント細胞よりも幼若な細胞に多く取り込まれていたが, HRPは幼若な細胞と成熟細胞との間に差はなかった。歯槽骨においてMPまたはHRPは, すべての骨小腔にみられ, セメント細胞と同様な骨細胞の細胞内小器官にみられた。特にHRPは骨基質最内側縁に強く沈着し, さかんに骨細胞に取り込まれていた。これらの結果よリセメント質と骨内の主な物質輸送経路はpericellular spaceの外側部分 (石灰化基質最内側縁) にあると思われ, セメント細胞は骨細胞と同様な代謝活性をもっているものと思われた。
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A rapid method for the preparation of highly purified cholinergic nerve endings from the electric organ of Torpedo is described. The endings retain their cytoplasmic components, as shown by biochemical and morphological observations. The homogeneity of these synaptosomes make them a useful tool for further studies.
Electric organ
Free nerve ending
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