|Author:||Michael K. Trower|
|Title:||In Vitro Mutagenesis Protocols (Methods in Molecular Biology)|
|Format:||docx txt lit lrf|
|ePUB size:||1291 kb|
|FB2 size:||1807 kb|
|DJVU size:||1864 kb|
|Publisher:||Humana Press; 1 edition (January 22, 1996)|
PDF In vitro mutagenesis is a major tool used by molecular biologists to make connections between nucleotide sequence and sequence function. In the post-genome era, in vitro mutagenesis is being used to establish the function of components of the proteome . Methods in Molecular Biology, Volume 182; In Vitro Mutagenesis Protocols. Book · January 2002 with 68 Reads.
No part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise without written permission from the Publisher. This publication is printed on acid-free paper.
Immunochemical Protocols. Page ii. Methods in molecular biology.
Site-directed protocols include those based on strand selection, PCR (including "splicing by overlap extension" and the "megaprimer" procedure), the ligase chain reaction, positive antibiotic selection, unique restriction site elimination, gapped heteroduplex formation, and solid-phase capture with the biotin/strepavidin system.
Glaxo-Wellcome, Hertfordshire, . Manual of specific mutagenesis protocols for both site-directed and random mutagenesis. Plastic comb spiral binding. 64 contributors, 47 . In Vitro Mutagenesis Protocols (Methods in Molecular Biology).
Methods in Molecular Biology. itself both in vivo and in vitro; and direct measurement of the activity of NO synthase. In addition, a number of i s s u e ~ u c has the use NO donors, peroxynitrite, and NO gas to mimic endogenous NO productiowhave been included, together with chapters on the use of inhibitors of NO synthase and the measurement of nitrotyrosine residues in proteins,on DNA damage, and on apoptosis caused by NO production. At present, the basic structural characterization of the oxygenase region is in a relatively early stage, consisting mainly of some mutagenesis studies. In all three isoenzymes, mutation of a certain cysteine residue (C415 in nNOS, C184 in eNOS, and C194 in iNOS) resulted in the loss of heme binding (37–39).
pp 374. Humana Press, Totowa, New Jersey.