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Advanced Methods in Protein Sequence Determination by Professor Saul B. Needleman (auth.)

By Professor Saul B. Needleman (auth.)

Confusion now hath made his masterpiece Macbeth II iii seventy two Whence and what are these execrable form? Paradise misplaced Ib 1 681 Confusion worse confounded Paradise misplaced Ib 1 995 while the manuscript for the 1st a part of this e-book was once proposed, it was once expected that the dialogue of the complete box of protein se­ quencing should be lined in one quantity - from purification and characterization of the protein via fragmentation by means of chemical or enzymic ability and, eventually, to reassembly of the pointed out person peptides into the reconstructed overall series. It quickly grew to become obvious that this could now not be attainable. whereas the purpose was once to limit the disclose of strategies purely to that info considering "hands on" rainy chemistry, it grew to become obvious thorough presentation will require, moreover, a dialogue of definite instrumental and extra theoretical techniques now not incorporated within the first quantity. additionally, the full realizing of the sphere of protein sequencing has complicated noticeably because the inception of this ebook. the aim of the 1st quantity used to be to supply functional info in adequate element to allow the researcher to adopt the particular sequencing systems in his personal laboratory.

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In fact, because the enzyme activity tends to become less stable with increasing purification, it is usually undesirable to carry the purification further. On the other hand, complete characterization of the enzyme necessitates purer material, and a Buchler Polyprep gel electrophoresis can be usefully employed at this stage. 4. Suitable stabilizing agents must be added to the system; in particular, thioglycollate is substituted for mercaptoethanol. The active pools from these electrophoresis runs exhibit two bands when examined on analytical gel electrophoresis and are about 200-fold purified relative to starting crude extracts (21).

6-10) are also better nucleophiles than aryl amino groups. For these reasons the TETA resin gives superior results in coupling carboxyl-activated peptides. For the combined coupling method, a support such as the EDAA-resin would probably give best results since it has both aryl and aliphatic amino groups. This, however, remains to be tested. After the peptide has attached to the support, excess resin amino groups are blocked, usually by reaction with methyl isothiocyanate. The resulting resin methylthiourea is somewhat unstable to acid, with the result that some decomposition products are noted during phenylthiohydantoin (PTH) analysis.

A third example is provided by lobster glyceraldehyde-3-phosphate dehydrogenase, a 333-residue protein containing 10 methionine residues (Fig. 18). Since the N-terminal of the protein is acetylated (105), sequencing of the intact protein is precluded. The five smaller peptides (3-23 residues) can be sequenced directly, the two containing 31 residues and that with 56 residues using the strategies discussed above. These procedures should yield about 60% of the sequences of the N-blocked peptide, and of the 50- and 69-residue peptides.

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