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This study presents the results of performance evaluations of the Cell-Dyn Sapphire (CD-Sapphire) undertaken by 3 study sites in Europe. These studies focused on the routine blood count analyses with specific consideration of precision and imprecision, linearity, inter-instrument correlations, and white blood cell differential and flagging efficiencies. The CD-Sapphire was compared to the Cell-Dyn CD4000, Bayer Advia 120, Beckman Coulter GenS, and reference microscopy.

Temperature and mash thickness are shown to affect both mash performance and enzyme activity. Alpha amylase was found to be considerably more resistant to heat inactivation than was beta amylase. This difference was reflected by changes in wort fermentability that were manifest at temperatures below those which affected levels of extract. Increasing the mashing temperature from 65°C to 80°C had only a slight effect on extract but reduced wort fermentability from over 70% to less than 30%. At 85°C and over, when temperature had a significant effect on alpha amylase, as well as on beta-amylase, extract was lost and starch was present in the wort. Diluting the mash with liquor had a similar effect to that of increasing temperature on both the amylolytic enzymes and on the mash performance. Thin mashes contained more starch and fewer fermentable sugars than did thick mashes at the same temperature. These changes can be related to the stability of the amylolytic enzymes.

The deletion plasmids, pRBH1 (1.5 MDa, kanamycin resistance, Kmr) and pUB110dB (1.5 MDa, Kmr), were obtained from pTB913 (2.9 MDa, Kmr, isolated from a thermophilic bacillus) and pUB110 (3.0 MDa, Kmr, from Staphylococcus aureus), respectively. All the nucleotide sequences of these deletion plasmids were determined. Replication origin regions of pRBH1 and pUB110dB contained, respectively, 63 base-pair inverted repeat and a large open reading frame, encoding RepB protein (235 amino acid residues). The nucleotide sequences were identical to each other except for one base in the center of the inverted repeat. Two copy number mutant plasmids, pRBHC3 and pRBHC7, were obtained from pRBH1. The mutation points were located at different positions in the RepB protein coding region (Gly to Asp for pRBHC3 and Gly to Glu for pRBHC7). RepB protein was shown to be involved in the copy number control of these plasmids.