Pub Date : 2000-05-01DOI: 10.1016/S0307-4412(00)00005-4
Norbert Latruffe, Shawn J. Hassell
Peroxisome proliferation in rodent liver is a good biochemical marker of toxicology for several classes of xenobiotics, including fibrates; phthalates and adipates; or chlorophenoxy-acetate, a herbicide. Research in peroxisomes provides a good example of the integration of fields related to basic sciences and biomedical and industrial health. A 25 min video programme illustrates techniques involved in the characterization of purified peroxisomes (Fig. 1
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Fig. 1. Electron microscope view of isolated peroxisomes (from rat liver ×50 000).
) and membranes, immunoblotting, measurement of proliferation markers, mRNA analysis at the post-transcriptional level, DNA techniques, cell cultures as biological models and computer analysis. It is aimed at undergraduates and non-biochemist advanced students in biology.
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Pub Date : 2000-05-01DOI: 10.1016/S0307-4412(00)00027-3
J.M. Wallach
{"title":"Workshop on teaching of biochemistry in Europe","authors":"J.M. Wallach","doi":"10.1016/S0307-4412(00)00027-3","DOIUrl":"10.1016/S0307-4412(00)00027-3","url":null,"abstract":"","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 3","pages":"Pages 139-140"},"PeriodicalIF":0.0,"publicationDate":"2000-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(00)00027-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56596271","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}
Pub Date : 2000-05-01DOI: 10.1016/S0307-4412(99)00145-4
V.H. Mulimani, G.N. Patil, Ramalingam
A laboratory practical experiment in Biotechnology involving the investigation of α-amylase production by solid state fermentation of Gibberella fujikuroi is described.
介绍了一项研究藤黑赤霉素固态发酵生产α-淀粉酶的生物技术实验室实践实验。
{"title":"α-Amylase production by solid state fermentation: a new practical approach to biotechnology courses","authors":"V.H. Mulimani, G.N. Patil, Ramalingam","doi":"10.1016/S0307-4412(99)00145-4","DOIUrl":"https://doi.org/10.1016/S0307-4412(99)00145-4","url":null,"abstract":"<div><p>A laboratory practical experiment in Biotechnology involving the investigation of <em>α</em>-amylase production by solid state fermentation of <em>Gibberella fujikuroi</em> is described.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 3","pages":"Pages 161-163"},"PeriodicalIF":0.0,"publicationDate":"2000-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00145-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92143307","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}
Pub Date : 2000-05-01DOI: 10.1016/S0307-4412(99)00091-6
José Carlos Cameselle, Alicia Cabezas, José Canales, Marı́a Jesús Costas, Ángeles Faraldo, Ascensión Fernández, Rosa Marı́a Pinto, João Meireles Ribeiro
This article describes a `dry-laboratory’ practical in which the multi-step purification of an enzyme is simulated. It has been devised to be implemented with beginner undergraduates taking an introductory course in biochemistry, with the aim of giving them a glimpse of the intensity of effort involved in complex, research-oriented experiments. The purification steps simulated are: preparation of a liver soluble extract, ammonium sulfate fractionation, gel filtration, ion-exchange and dye-ligand affinity chromatography. Before the simulation, our students are familiar with the preparative and analytical techniques involved, through short `cookbook’ laboratory experiments and, in some cases, ad hoc demonstrations. For the simulation, the students are given detailed protocols of the preparative and analytical experiments, and the raw numeric or graphical data obtained. They have to perform the calculations and graphing necessary to produce a purification table. The 27-page Student Booklet needed to implement the practical is offered by the authors to interested teachers, as a printable electronic file.
{"title":"The simulated purification of an enzyme as a `dry’ practical within an introductory course of biochemistry","authors":"José Carlos Cameselle, Alicia Cabezas, José Canales, Marı́a Jesús Costas, Ángeles Faraldo, Ascensión Fernández, Rosa Marı́a Pinto, João Meireles Ribeiro","doi":"10.1016/S0307-4412(99)00091-6","DOIUrl":"https://doi.org/10.1016/S0307-4412(99)00091-6","url":null,"abstract":"<div><p>This article describes a `dry-laboratory’ practical in which the multi-step purification of an enzyme is simulated. It has been devised to be implemented with beginner undergraduates taking an introductory course in biochemistry, with the aim of giving them a glimpse of the intensity of effort involved in complex, research-oriented experiments. The purification steps simulated are: preparation of a liver soluble extract, ammonium sulfate fractionation, gel filtration, ion-exchange and dye-ligand affinity chromatography. Before the simulation, our students are familiar with the preparative and analytical techniques involved, through short `cookbook’ laboratory experiments and, in some cases, ad hoc demonstrations. For the simulation, the students are given detailed protocols of the preparative and analytical experiments, and the raw numeric or graphical data obtained. They have to perform the calculations and graphing necessary to produce a purification table. The 27-page Student Booklet needed to implement the practical is offered by the authors to interested teachers, as a printable electronic file.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 3","pages":"Pages 148-153"},"PeriodicalIF":0.0,"publicationDate":"2000-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00091-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136521743","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}
The College of Medicine, King Khalid University of Abha, Saudi Arabia currently accepts 100 students a year, up from 50 to 70 students four years ago. The first-year students take four science courses (Biology,Chemistry, Physics, and Statistics) in addition to some general university requirement courses. Biochemistry is offered in the second year, Anatomy in the second and third year and Pharmacology in the fourth year. This study was carried out to determine the correlation between the performance of medical students in Biochemistry and their performance in Anatomy and Pharmacology. Data were obtained from two groups of students (Group 22 and 23) of the years 1995 and 1996 who had already taken Biochemistry, Anatomy and Pharmacology. Performance was equal in Pharmacology but in biochemistry performance of group 23 was clearly lower than group 22. Scores of students in Biochemistry course strongly correlated with the basic Pharmacology course (r=0.714, P<0.0001). Scores in Anatomy also correlated with those in Biochemistry (r=0.616, P<0.001) but much less with scores in Pharmacology (r=0.345, P<0.01).
沙特阿拉伯阿卜哈国王哈立德大学医学院目前每年招收100名学生，而四年前每年招收50至70名学生。一年级的学生除了一些普通的大学必修课程外，还要修四门科学课程(生物、化学、物理和统计学)。第二年开设生物化学课程，第二年和第三年开设解剖学课程，第四年开设药理学课程。本研究旨在探讨医学生生物化学成绩与解剖学、药理学成绩的相关性。数据来自1995年和1996年两组已经修过生物化学、解剖学和药理学的学生(22组和23组)。23组的药理学性能与22组相当，但生物化学性能明显低于22组。学生生物化学课程成绩与药理学基础课程成绩呈显著正相关(r=0.714, P
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Cameselle, Cabezas, Canales, Jesús Costas M, Faraldo, Fernández, María Pinto R, Meireles Ribeiro J
This article describes a 'dry-laboratory' practical in which the multi-step purification of an enzyme is simulated. It has been devised to be implemented with beginner undergraduates taking an introductory course in biochemistry, with the aim of giving them a glimpse of the intensity of effort involved in complex, research-oriented experiments. The purification steps simulated are: preparation of a liver soluble extract, ammonium sulfate fractionation, gel filtration, ion-exchange and dye-ligand affinity chromatography. Before the simulation, our students are familiar with the preparative and analytical techniques involved, through short 'cookbook' laboratory experiments and, in some cases, ad hoc demonstrations. For the simulation, the students are given detailed protocols of the preparative and analytical experiments, and the raw numeric or graphical data obtained. They have to perform the calculations and graphing necessary to produce a purification table. The 27-page Student Booklet needed to implement the practical is offered by the authors to interested teachers, as a printable electronic file.
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Pub Date : 2000-05-01DOI: 10.1016/S0307-4412(99)00148-X
M.I Arufe, J.L Romero, J.J Gamero, M.J Moreno
A simple undergraduate laboratory experiment that can be used in Biochemistry and Toxicology courses to illustrate the importance of metabolic reactions in the toxicity of chemical substances is reported. It involves the experimental confirmation that oxidized phosphorothionate esters, commonly used as insecticides, are stronger cholinesterase inhibitors and therefore exhibit higher toxicity than do their sulphur analogs starting from which the first are formed by in vivo oxidative desulphuration. Two separated aliquots of a bovine blood sample are incubated with parathion and paraoxon, its oxygen analog, and compared for cholinesterase activity with “normal” blood. Previously, a standard sample of paraoxon was obtained by oxidation of the thiono group of parathion with bromine vapour by reaction TLC. The comparison of the inhibitory capacity of both compounds is made by a colorimetric procedure using acetylthiocholine as substrate of the enzyme and 5,5′-dithiobis-(2-nitrobenzoic acid) as chromogen.
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