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Lysozyme recombinant

Fig. 6 Transition temperature of protein unfolding measured by CE and CD. Proteins lysozyme from chicken egg (LYS), a-lactalbumin from human milk (LAL-h), a-lactalbumin type III from bovine milk (LAL-III), cytochrome c from bovine heart (CYT), recombinant dihydrofolate reductase (DHFR). Fig. 6 Transition temperature of protein unfolding measured by CE and CD. Proteins lysozyme from chicken egg (LYS), a-lactalbumin from human milk (LAL-h), a-lactalbumin type III from bovine milk (LAL-III), cytochrome c from bovine heart (CYT), recombinant dihydrofolate reductase (DHFR).
AOT/isooctane [304],refolding of recombinant proteins such as lysozyme [305], and refolding studies on triosephosphate isomerase using fluorescence resonance energy transfer [306]. [Pg.171]

It has been suggested that the exons could correspond to functional units of proteins and that new proteins could have evolved by the recombination of different exons.27 Early circumstantial evidence was consistent with this idea. For example, hen egg white lysozyme DNA contains four exons. Exon 2 has the... [Pg.27]

Ref. 12 describes the preparation of microspheres of lysozyme, insulin, albumin, and recombinant human deoxyribonuclease. Of these proteins, insulin powders demonstrated the highest degree of agglomeration. [Pg.173]

Assays for Copy Number, Differential Expression, and Recombination in Lysozyme Multigene Family... [Pg.552]

The molecular mechanisms by which the extension of the N-terminus by the extra methionine residue destabilized recombinant a-lactalbumin remain unclear. Additional conformational entropy of the extra methionine residue in the unfolded state could account for the destabilization and unfolding-rate acceleration of the recombinant protein [22]. Ishikawa and coworkers reported the destabilization of recombinant bovine a-lactalbumin, similarly induced by the extra N-terminal methionine residue, and showed that the enthalpy change of thermal unfolding was the same for the authentic and recombinant proteins, indicating that the destabilization was caused by an entropic effect [42]. However, the destabilization by the extra methionine residue in the lysozyme homologous to a-lactalbumin was rather enthalpic and accompanied by a disruption of hydrogen-bond networks in the N-terminal region [43,44]. [Pg.18]

BSA monomer, ovalbumin (chicken), P-lactoglobulin (bovine milk), serum albumin (human), carbonic anhydrase (bovine), L-glutamic dehydrogenase (bovine liver), a-chymotrypsin (bovine), a-chymotrypsinogen A (bovine), immunoglobulin (bovine milk), pepsin, trypsin (bovine), and heparin were from Sigma. RNase and lysozyme (egg white) were from Calbiochem. The recombinant human basic fibroblast... [Pg.115]

Recombinant bovine somatotropin, lysozyme Both the excipient type (sucrose, sorbitol, glycerol) and moisture content affected protein degradation [30]... [Pg.1649]

Ventria is producing rhLF and recombinant human lysozyme (rhLZ) accumulating in rice seed at a level of 5 g kg flour weight [382]. Rice-derived rhLF and rhLZ were shown to be identical to the human proteins, and to have stability similar to native human lactoferrin and lysozyme when exposed to heat, pH changes, and in vitro digestion [308, 314, 383]. Both lactoferrin and lysozyme are multifunctional... [Pg.867]

California-based Ventria Bioscience (Sacramento) is at the stage of field trials of transgenic rice plants expressing recombinant lactoferrin and lysozyme in rice seed (see Part IV, Chapter 8). It is worth mentioning, that these products might reach market later than planned considering difficulties with obtaining the necessary field trial permits [39-41]. [Pg.905]

To improve human lysozyme expression, we attempted to improve heterologous recombinant protein expression levels by 1) co-transformation of Gib and Gtl expression cassettes and 2) crossing of two independent transgenic lines expressing lysozyme protein from Gtl and Gib cassettes. These experiments failed to improve lysozyme expression. This implies that the gene transcription and copy number are... [Pg.936]


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