Hen egg albumin

Compound 62 is a glyco-asparagine of the oligomannoside type containing five Man residues that has been isolated from the urine of a patient with Gaucher s disease58,59 it was also obtained from hen-egg albumin.95 The 500-MHz, H-n.m.r. spectrum of 62 is presented in Fig. 45 its n.m.r. parameters are compiled in Table XXIV. 

Fig. 5. Quantitative precipitin reaction between crystalline hen egg albumin (Ea) and rabbit antibody (Ab) to crystalline hen egg albumin. From Heidelberger and Kendall. ...

Different formulations of saponin-adjuvanted vaccines were tested for humoral and cell-mediated responses in mice. Many antigens, often including hen egg albumin (ovalbumin, OVA) as the antigen to be tested, have been used for immunizations, enzyme immunoassays, antigen-specific CTL and cellular proliferation assays [31]. 

These experiments demonstrate that the group of genes governing antibody synthesis regulates the production of antibody molecules belonging to the two main classes of Ig. The study of the antibody response to other protein antigens hen egg albumin, BSA and DNP-BGG have confirmed the preceding conclusion and extended these results to the other classes and sub-classes of antibody previously mentioned. 

It is now clear that the molecular weight of cathepsin D from a variety of sources is close to 42,000 (3-7). The elution volume in gel chromatography is typically identical with that of hen egg albumin, and it is unclear why higher values (50,000 - 60,000) were obtained in some of the earlier work. 

Squaraine dyes 10b, 39a, 39b, 41a, 41c, 41d, and 41e were used to measure different proteins such as BSA, HSA, ovalbumin, avidin from hen egg white, lysozyme, and trypsin (Fig. 12) [58]. It is difficult to predict correlations between the dyes structures and the affinity or sensitivity of the dyes for different proteins. All squaraine probes exhibit considerable fluorescence increases in the presence of BSA. Dicyanomethylene-squaraine 41c is the brightest fluorescent probe and demonstrates the most pronounced intensity increase (up to 190 times) in presence of BSA. At the same time, the fluorescent response of the dyes 10b, 39a, 39b, 41a, 41c, 41d, and 41e in presence of other albumins (HSA and ovalbumin) is, in general, significantly lower (intensity increases up to 24 times). Dicyanomethylene-squaraine 41a and amino-squaraines 39a and 39b are the most sensitive probes for ovalbumin. Dyes 41d, 10b, and 41e containing an A-carboxyalky I -group demonstrate sufficient enhancement (up to 16 times) in the presence of avidin. Nevertheless, the presence of hydrolases like lysozyme or trypsin has only minor effects on the fluorescence intensity of squaraine dyes. 

Addition of amino-reduc-tones prepared from hex-oses and secondary amines Addition of mixture of glucose and Gly, more effective than either Addition of 0.02% MRP from glucose-Gly Wheat gliadin and hen s egg albumin Over cooking... 

The first systematic investigation of the binding of a metal ion by lysozyme is probably that by Fiess and Klotz (1952), who found the affinity of five proteins for Cu(ll) at pH 6.5 to be in the order bovine a-casein > /3-casein > serum albumin > /8-lactoglobulin > hen egg-white lysozyme. Soon afterward Carr (1953), using membrane electrodes, found that —0.7 mol of Ca(ll) was bound per mole of hen egg-white lysozyme at pH 7.4, compared with 6.7 mol of Ca(ll) per mole of bovine serum albumin. 

Figure 2. SDS gel electrophoresis of the products of partial cystine cleavage for several test proteins. A. molecular weight standards, B. yeast alcohol dehydrogenase. C. P-lactoglobulin, D. hen egg lysozyme, E. ovalbumin, F. calf fetal serum fetuin. Molecular weight standards are indicated by arrows on the left side of the gel and are bovine serum albumin (66,300), bovine liver glutamate dehydrogenase (55,400), porcine muscle lactate ddiydiogenase (36,500), bovine erythrocyte carbonic anhydrase (31,000), soybean trypsin inhibitor (21,500), hen egg lysozyme (14,400), bovine lung aprotinin (6,000), unresolved bovine pancreatic insulin A and B chains.

By direct absorption measurements, we have directly probed the low frequency collective motions of proteins in water by terahertz absorption spectroscopy. We have isolated, for the first time, the 0.075 - 3.72 THz absorption of bovine semm albumin " and hen egg white lysozyme in water, and made direct comparison with existing... 

For the construction of artificial metalloproteins, protein scaffolds should be stable, both over a wide range of pH and organic solvents, and at high temperature. In addition, crystal structures of protein scaffolds are crucial for their rational design. The proteins reported so far for the conjugation of metal complexes are listed in Fig. 1. Lysozyme (Ly) is a small enzyme that catalyzes hydrolysis of polysaccharides and is well known as a protein easily crystallized (Fig. la). Thus, lysozyme has been used as a model protein for studying interactions between metal compounds and proteins [13,14,42,43]. For example, [Ru(p-cymene)] L [Mn(CO)3l, and cisplatin are regiospecificaUy coordinated to the N = atom of His 15 in hen egg white lysozyme [14, 42, 43]. Serum albumin (SA) is one of the most abundant blood proteins, and exhibits an ability to accommodate a variety of hydrophobic compounds such as fatty acids, bilirubin, and hemin (Fig. lb). Thus, SA has been used to bind several metal complexes such as Rh(acac)(CO)2, Fe- and Mn-corroles, and Cu-phthalocyanine and the composites applied to asymmetric catalytic reactions [20, 28-30]. 

R. D. Marshall and A. Neuberger, Carbohydrates in protein. VIII. The isolation of 2-acet-amido l-(L-P-aspartamido)-l,2-dideoxy-p-D-glucose from hen s egg albumin. Biochemistry, 3 (1964) 1596-1600. 

In closing, we refer to the recent pubHcation [358] in which the synthesis of mesoporous poly-DVB and the characterization of its porous structure were reported. The polymer readily adsorbs another surrogate for P2M. lysozyme of hen egg white with molecular weight of 14 kDa and size of about 4nm, but exhibits a pretty low affinity to human serum albumin. At present, however, it is hard to evaluate whether there is any prospect of real application of the sorbent because no information is available on its hemocompatibihty. 

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