By Marshall Clagett
This quantity keeps Marshall Clagett's reports of a number of the facets of the technology of old Egypt. the amount provides a discourse at the nature and accomplishments of Egyptian arithmetic and in addition informs the reader as to how our wisdom of Egyptian arithmetic has grown because the ebook of the Rhind Mathematical Papyrus towards the top of the nineteenth century. the writer charges and discusses interpretations of such authors as Eisenlohr, Griffith, Hultsch, Peet, Struce, Neugebauer, Chace, Glanville, van der Waerden, Bruins, Gillings, and others. He additionally additionally considers reports of newer authors equivalent to Couchoud, Caveing, and Guillemot.
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Extra info for Ancient Egyptian Science, A Source Book. Volume Three: Ancient Egyptian Mathematics (Memoirs of the American Philosophical Society)
Excretion from gram-positive species such as B. subtilis sends the product into the culture medium, with little feedback limitation on total expression level. , and Soda, K. 1989. Overproduction of thermostable leucine dehydrogenase of Bacillus stearothermophilus and its one-step purification from recombinant cells of Escherichia coli. Biotechnol. Appl. Biochem. 11:307-316. M. 1990. Engineering proteins for purification. Trends Biotechnol. 8:88-93. P. ) 1990. Guide to protein purification. Methods Enzymol.
Additional Materials (also see Support Protocol 1) [8-14C]GTP (Amersham Pharmacia Biotech) 250:500:1 (v/v/w) Triton X-100/toluene/2,5-diphenyloxazole (PPO) Carry out Support Protocol 1 with the following modifications at the indicated steps. 4a. 7 µCi of [8-14C]GTP to the solution of unlabeled GTP before periodate oxidation. 7b. Determine radioactivity in a sample of the gel washings by scintillation counting in a mixture by scintillation counting in 250:500:1 Triton X-100/toluene/PPO. 1). 44 × 106 — a9 ml of 250:500:1 (v/v/w) Triton X-100:toluene:PPO were mixed with 1 ml of the aqueous phase and the radioactivity determined in a liquid scintillation counter.
Collect fractions (∼10 ml) and determine their A280 (see Basic Protocol 2), conductivity, and enzyme activities (see Basic Protocol 3). Pool the fractions containing glutamate dehydrogenase activity. Retain a small aliquot of this pooled material for determining protein concentration by the biuret procedure (Basic Protocol 2) and assaying GDH activity (Basic Protocol 3). The combined active fractions require concentration before the next step; this can be done either by ultrafiltration or ammonium sulfate precipitation.