Preparation of protein

King, P., Li, Y., and Kochoumian, L. (1978) Preparation of protein conjugates via intermolecular disulfide bond formation. Biochemistry 17, 1499. 

Zalipsky, S., Seltzer, R., and Nho, K. (1991) Succinimidyl carbonates of polyethylene glycol Useful reactive polymers for preparation of protein conjugates. In Polymeric Drugs and Drug Delivery Systems (R.L. Dunn, and R.M. Ottenbrite, eds.), pp. 91-100. American Chemical Society, Washington, D.C. 

The third approach (iii), the solid-phase synthesis, has not been yet implemented for the preparation of protein-like HP-copolymers with heterogeneous blockiness, although the possibility—inherent in this method—to form the macromolecular chains with a well-defined chemical sequence of monomeric units is of great interest for the problem. That is why, these possibilities will also be discussed briefly in Sect. 2.4. 

A general idea related to the preparation of protein-like copolymers through the co-polymerization or co-polycondensation of the mixtures of comonomers with differing hydrophilicity/hydrophobicity has been described in Sect. 2.1. Scheme 4 demonstrates the multi-step operations used in the first successful realization [26,27] of such an approach in a free radical polymerization process. 

Generally speaking, we should note that the synthetic potentials of the polycondensation approach for the preparation of protein-like copolymers are only now beginning to be explored. Nonetheless, even the first results show promising directions for future synthetic developments that can hardly be reached through the polymerization processes. 

We have observed that such proteins as CaM and bovine serum albumin (BSA) can be developed at the air-water interface to form monolayer protein films. In previous works, the developed BSA monolayer was stabilized by cross-linking with a bifunctional reagent immediately after the preparation of protein monolayer. The BSA thin film thus prepared can be employed as a passive material, e.g., an ultrathin protein film for a matrix of enzyme-linked immunosorvent assays. 

Defatted flours are especially attractive as protein sources, since 10-12% substitution of wheat flour with 50% protein flour will raise total protein content of typical wheat breads by approximately 50%, and 25% substitution will almost double the protein content of cookies. Preparation of protein-enriched breads has been reported in the literature using soy flours and protein concentrates (25), peanut flours and peanut protein concentrates C26, 27), glandless cottonseed flours, concentrates and isolates (28), sunflower seed flours and seed protein concentrates (27) and sesame flours and protein concentrates (26). 

When urea-denatured preparations of protein Lll are introduced into physiological buffers, two different conformations occur as shown by NMR studies (Kime et al., 1980). One form is distinctly folded while... 

Roth, J. (1982) The preparation of protein A-gold complexes with 3 nm and 15 nm gold particles and their use in labeling multiple antigens on ultra-thin sections. Histochem. J. 14,791-801. 

John H. Northrop United States preparation of proteins and enzymes in... 

The IC, values of the vinca binary alkaloids for microtubule assembly were measured from their concentration-dependent effects on steady-state turbidity levels. Values are presented from two separate experiments. The products induced by a high concentration (10 M) of each compound with MTP or steady-state microtubules assembled from MTP were determined by transmission electron microscopy of steady-state solutions from at least two separate preparations of protein with similar results. SA, Spiral aggregates S, single spirals Am. amorphous aggregates MT, microtubules N.D., not determined. 

Finally, an understanding of the making of a microarray is fundamentally important to those interested in producing "spotted" arrays and properly using them. While complementary (cDNA) microarray fabricahon on glass slides has been well studied, we have less experience with the attachment of oligonucleotides and the preparation of protein arrays. Moreover, additional substrates and surface chemistries that may be better suited for printing proteins are now available. 

Dent AH, Aslam M (1999) The preparation of protein-protein conjugates. In Aslam M, Dent AH (eds.) Bioconjugation. Protein coupling techniques for the biomedical sciences. Macmillan Reference Ltd., London,... 

The preparation of protein-rich morama flours follows a number of simple unit operations. These include heating, dehulling, defatting (in some cases), and milling (Fig. 5.5). These operations may impact either... 

Chu, B.S., Ichikawa, S., Kanafusa, S., Nakajima, M. (2007). Preparation of protein-stabilized p-carotene nanodispersions by emulsification-evaporation method. Journal of the American Oil Chemists Society, 84, 1053-1062. 

If precast gels are provided, move ahead to the preparation of protein samples for electrophoresis. If gels are to be made, follow these instructions for preparation of an SDS gel of 12% acrylamide. 

It is necessary to make high-titer stocks of the recombinant phage for the generation of stocks of phage to work with on a day-to-day basis, and also for the preparation of DNA for sequencing or for the preparation of protein lysates from recombinant phage. A relatively quick and easy method for the preparation of high-titer lysates is described below. 

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