Preparative biochemistry最新文献_第2页

Fractionation and characterization of two forms of peroxidase from Oryza sativa. 水稻中两种过氧化物酶的分离与特性研究。

Preparative biochemistry Pub Date : 1995-02-01 DOI: 10.1080/10826069508010104

A Padiglia, R Medda, G Pazzaglia, A Rescigno, E Cruciani, G Floris

{"title":"Fractionation and characterization of two forms of peroxidase from Oryza sativa.","authors":"A Padiglia, R Medda, G Pazzaglia, A Rescigno, E Cruciani, G Floris","doi":"10.1080/10826069508010104","DOIUrl":"https://doi.org/10.1080/10826069508010104","url":null,"abstract":"Peroxidase (E.C. 1.11.1.7., hydrogen donor oxidoreductase) is widely distributed and has been isolated from many higher plants (1). The wide distribution of the enzyme suggests that it could be of great biological importance. However the role that it plays in metabolism is not clear due to the large number of reactions it catalyzes and the considerable number of isozymic species (2). In tomato plants, Evans and Aldridge (3) separated out six isoperoxidases and in a later paper Evans reported 12 isoperoxidases from tomato shoots (4). A homogeneous tomato fruit peroxidase isozyme was obtained by Jen et al. (5) using hydrophobic chromatography. Isozymes were not detected in Euphorbia characias peroxidase (6), in Ipomoea batatas peroxidase (7) and in Hordeum vulgare peroxidase (8). The simultaneous presence of Cu (II) amine oxidase and peroxidase in cell walls suggests that the peroxide generated on oxidation of the amines could be utilized by the peroxidase (6,8,9). In the graminea Oryza sativa, widely distributed, an FAD amine oxidase is present that oxidizes diamines (10). In this plant we also found two isoperoxidases called perox I and II. Only perox I was purified to homogeneity and its enzymatic, physical and chemical properties have been studied.","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"25 1-2","pages":"11-9"},"PeriodicalIF":0.0,"publicationDate":"1995-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069508010104","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18609943","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

A simple technique for the purification of plasma membranes from ejaculated boar spermatozoa. 一种纯化猪精质膜的简单技术。

Preparative biochemistry Pub Date : 1995-02-01 DOI: 10.1080/10826069508010108

G C Althouse, K A Bruns, L E Evans, S M Hopkins, W H Hsu

引用次数: 10

Purification and characterization of an NAD(P)H:quinone oxidoreductase from Glycine max seedlings. 最大甘氨酸幼苗中 NAD(P)H:quinone 氧化还原酶的纯化和表征。

Preparative biochemistry Pub Date : 1995-02-01 DOI: 10.1080/10826069508010107

A Rescigno, F Sollai, S Masala, M C Porcu, E Sanjust, A C Rinaldi, N Curreli, D Grifi, A Rinaldi

引用次数: 11

An improved SDS-polyacrylamide gel electrophoresis for resolution of peptides in the range of 3.5-200kDa. 改进的sds -聚丙烯酰胺凝胶电泳可分离3.5-200kDa范围内的多肽。

Preparative biochemistry Pub Date : 1995-02-01 DOI: 10.1080/10826069508010103

Z Khalkhali-Ellis

引用次数: 22

Identification, characterization, and partial purification of glucoamylase from Aspergillus niger (syn A. ficuum) NRRL 3135. 黑曲霉(Aspergillus niger, syn A. ficuum) NRRL 3135中葡萄糖淀粉酶的鉴定、表征和部分纯化。

Preparative biochemistry Pub Date : 1995-02-01 DOI: 10.1080/10826069508010106

A S Vandersall, R G Cameron, C J Nairn, G Yelenosky, R J Wodzinski

引用次数: 17

Improved large-scale purification of transducin, and its alpha and beta gamma subunits from frozen retinas. 改进了从冷冻视网膜中大规模纯化转导蛋白及其α和β γ亚基的方法。

Preparative biochemistry Pub Date : 1994-11-01 DOI: 10.1080/10826069408010099

R E Jonas, C Yuan, T G Ebrey

引用次数: 1

Fast purification of Phaseolus vulgaris isolectins. 菜豆分离素的快速纯化。

Preparative biochemistry Pub Date : 1994-11-01 DOI: 10.1080/10826069408010091

E Zenteno, M Ortega, Z Qin, J Montreuil, H Debray

引用次数: 3

Purification of rat liver glucokinase. 大鼠肝葡萄糖激酶的纯化。

Preparative biochemistry Pub Date : 1994-11-01 DOI: 10.1080/10826069408010095

Y Toyoda, I Miwa, M Kamiya, S Ogiso, J Okuda

引用次数: 1

Fractionation of rat liver tRNA by reversed-phase high performance liquid chromatography: isolation of Iso-tRNAs(Pro). 反相高效液相色谱法分离大鼠肝脏tRNA:分离iso -tRNA (Pro)。

Preparative biochemistry Pub Date : 1994-11-01 DOI: 10.1080/10826069408010090

D Kanduc

引用次数: 7

Purification and characterization of triokinase from porcine kidney. 猪肾三磷酸激酶的纯化及特性研究。

Preparative biochemistry Pub Date : 1994-11-01 DOI: 10.1080/10826069408010094

I Miwa, Y Kito, J Okuda

{"title":"Purification and characterization of triokinase from porcine kidney.","authors":"I Miwa, Y Kito, J Okuda","doi":"10.1080/10826069408010094","DOIUrl":"https://doi.org/10.1080/10826069408010094","url":null,"abstract":"In order to be able to use triokinase for the enzymatic assay of tissue glyceraldehyde, we purified the enzyme to homogeneity from porcine kidney and characterized its biochemical properties. The purification was performed by polyethylene glycol fractionation, anion exchange chromatography, hydroxyapatite chromatography, hydrophobic chromatography, and gel filtration. The enzyme was purified 937-fold from the crude extract with an overall yield of 28%. It had a molecular weight of 122,000 and was a dimer composed of identical subunits. The optimal pH and optimal temperature were 7.0 and 60 degrees C, respectively. This enzyme was stable when incubated at pH 7.0 at 40 degrees C for 1 h in the presence of 0.1 mg/ml bovine serum albumin. No loss of activity occurred for at least 1 month when the enzyme was stored at 4 degrees C in the presence of 1 mM dithiothreitol and 15 mM NaN3 under N2. Only three compounds, i.e., D-glyceraldehyde, dihydroxyacetone, and glycolaldehyde, acted as the substrate of the enzyme, having Km's of 11, < 5, and 260 microM, respectively. The Km for ATP-Mg2+ was 68 microM. These results indicate that porcine kidney triokinase has properties advantageous for the glyceraldehyde assay using glyceraldehyde-3-phosphate dehydrogenase as a coupling enzyme.","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"24 3-4","pages":"203-23"},"PeriodicalIF":0.0,"publicationDate":"1994-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069408010094","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18831849","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6