Albumin evolution

Maxson LR, Highton R, Wake DB (1979) Albumin evolution and its phylogenetic implications in the plethodontid salamander genera Plethadon and Ensatina. Copeia 1979 502-508... 

FIGURE 5.2 Clinical outcome of patients in the double-blind, proof-of-concept trial evaluating EPO in acute stroke, (a) Barthel Index (rhEPO vs. placebo, p < 0.05). (b) Modified Rankin Scale (rhEPO vs. placebo, p < 0.07) on day 30. Dead patients received the worst possible score. Evolution of lesion size of patients in the efficacy trial of Albumin in acute stroke, ((a-1) and DWI and (a-2) FLAIR.) (Reprinted with permission from reference 50.)... 

Control experiments verified that the neuraminidase active site was responsible for controlling DCL evolution. First, substitution of neuraminidase with bovine serum albumin as the target produced no amplification at all. Second, reconstituting the DCL in the presence of excess zanamivir, a commercially available potent inhibitor of neuraminidase, likewise gave results identical to the blank DCL in the absence of any target. 

Experiments were performed using capsules with membranes made of covalently linked human serum albumin (HSA) and alginate [7, 8], Details are given in [4], Figure 2 shows the evolution of a capsule after removal at time I, 0 from a solution of NaCl at 11 g/1 and immersion in a solution at 3.5 g/1. The experimental results fit well to a single exponential, leading to an estimate for D [3],... 

Harper ME, Dugaiczyk A. Linkage of the evolution-arily-related serum albumin and a-fetoprotein genes within qll-22 of human chromosome 4. Am J Hum Genet 1983 35 565-72. 

Comparison of sequences of the same protein in different species yields a wealth of information about evolutionary pathways. Genealogical relations between species can be inferred from sequence differences between their proteins. We can even estimate the time at which two evolutionary lines diverged, thanks to the clocklike nature of random mutations, For example, a comparison of serum albumins found in primates indicates that human beings and African apes diverged 5 million years ago, not 30 million years ago as was once thought. Sequence analyses have opened a new perspective on the fossil record and the pathway of human evolution. 

A reaction system consisting of a Fe(II) salt, BSA, Ne2S, and 2-mer-captoethanol afforded a dark brown solution whose absorption spectrum ( max 420 nm) had the appearance of a [4Fe-4S] + cluster (96). Formation of additional BSA-bound Fe-S species cannot be discounted, however. The albumin-cluster protein showed weak hydrogenase activity in the form of dihydrogen evolution in the presence of reduced methyl viologen (96). The protein was not further characterized. 

In thylakoids the pattern of proton release into the lumen can be measured with neutral red as indicator and bovine serum albumin as membrane impermeable buffer of the bulk phase (2). With reaction centre complexes both the donor and the acceptor side of PS II are exposed to the dye. Therefore, selective buffering is impossible and it makes no difference whether one uses membrane adsorbed dyes, like neutral red, or hydrophilic ones, like bromo-cresol purple. In fact, both dyes showed the same extent and also the same kinetics of proton release. We prefered to use bromo-cresol purple which pK (6.2) is in the range of the pH-optimum for O2 evolution by reaction centre complexes. Whether we used ferricyanide alone or in combination with 2,5-Dichloro-p-benzoquinone as terminal electron acceptor, had only little effect on the signal. That ferricyanide here acted as acceptor for the PS II reaction centre complexes is demonstrated by fig. 2.. 

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