Methylated albumin

In addition to the above, there are emulsion and suspension stabilizers that act as protective colloids and in some cases as thickeners gums (such as acacia and traga canth), alginates, starch and starch derivatives, casein, glue, egg albumin, methyl cellulose, hydrated Mg and Al silicates, etc Refs Same as in previous item... 

Talsky 1978 3 Spectra of RNase, y-globulin, serum albumin, fibrinogen, aldolase, cytochrom c, hen albumin, methylated hen albumin 108... 

This experiment provides a nice example of the application of spectroscopy to biochemistry. After presenting the basic theory for the spectroscopic treatment of protein-ligand interactions, a procedure for characterizing the binding of methyl orange to bovine serum albumin is described. 

Methyl paraoxon may also be made unavailable by binding to noncritical tissue and plasma constituents (Benke and Murphy 1975), including cholinesterase (Parkinson 1996). In addition, the parent compound is bound to albumin, in serum, as discussed previously in Section 3.4.2.4, but this binding does not appear to limit the availability of methyl parathion to the tissues, indicating that it is reversible. Tissue binding appears to be more important than serum binding (Braeckman et al. 1980, 1983). 

Data from a single study in dogs suggest that hepatic first-pass metabolism may limit systemic availability of the parent compound following oral exposure (Braeckman et al. 1983). Placental transfer of methyl parathion was demonstrated in pregnant rats 1-3 days before parturition. Thirty minutes after administration, both methyl parathion and methyl paraoxon were found in fetal brain, liver, and muscle methyl parathion, but not methyl paraoxon, was detected in placenta and maternal liver (Ackermann and Engst 1970). Methyl parathion binds reversibly to serum albumin, but is readily distributed to the tissues (Braeckman et al. 1980, 1983). 

GME glycine methyl ester GDM glutamic dimethyl ester EDA ethylendiamine GAM glucosamine HDA hexadecylamine BSA bovine serum albumin OVA ovalbumin CA carbonic anhydrase MYO myoglobin H alkaline hydrolysis for converting ester groups from GME or GDM into free carboxylic acid groups that were subsequently activated with EDC for further modifications. 

MARCKS Myristolated, alanine-rich C kinase substrate specific protein kinase C substrate MBP Major basic protein MBSA Methylated bovine serum albumin... 

Pandurangi, R.S. et al. (1995b) High efficiency photolabeling of human serum albumin and human g-globulin with [14C]Methyl 4-azido-2,3,5,6-tetrafluorobenzoate. Bioconjugate Chem. 6, 630-634. 

Protein (animal hydrolysates, zein, albumin) (3) Methyl cellulose derivatives (3)... 

Methyl orange buffered at pH 3.5 binds to albumin with greater affinity than to other proteins and the resulting complex shows reduced absorbance at 550 nm. The method is unsuitable as a general method for protein determination because of considerable variation in the binding of the dye with different proteins. 

Recent studies with quinoline-4-carboxylic acid angiotensin II receptor antagonists have confirmed the interest of (oxodioxolyl)methyl esters as prodrugs with improved oral bioavailability and efficacy in laboratory animals [79], Olmesartan, another angiotensin II receptor antagonist, has also been derivatized to a (5-methyl-2-oxo-l,3-dioxol-4-yl)methyl carboxylate designated as olmesartan medoxomil [80], In this case, both human serum albumin and arylesterase (presumably EC 3.1.1.2, although paraoxonase cannot be excluded) were shown to be involved in hydrolysis. 

Fig. 4. Extent of binding of methyl orange at pH 7.0 and 25°C as a function of free (nonbound) dye concentrations (1) polyethylenimine with 8.4% of residues acylated by lauroyl groups (2) polyethylenimine with 11.5% of residues acylated by hexanoyl groups (3) polyethylenimine with 10% of residues acylated by butyrl (O) or isobutyrl ( ) groups (4) Polyethylenimine, PEI-600 (5) bovine serum albumin.

The enantioselective oxidation of prochiral sulfides with DMD has been achieved by using bovine serum albumin (BSA) as the chiral inductor Moderate to good enan-tioselectivities have been reported in the presence of this protein, for which a typical example is shown in equation 22 . As yet, however, no enantioselective oxidation of a prochiral sulfide has been documented by employing an optically active dioxirane. We have tried the enantioselective oxidation of methyl phenyl sulfide with the dioxirane generated from the ketone 7 (Shi s ketone), but an ee value of only ca 5% was obtained. One major hurdle that needs to be overcome with such enantioselective dioxirane oxidations is the suppression of the background oxidation of the sulfide substrate by Caroate, an unavoidable feature of the in-situ mode. 

Fig. 12.1.4 Immobilization of bovine serum albumin on colloidal silica grafted with poly (maleic anhydride-styrene) (O), poly(maleic anhydride-methyl methacrylate) ( ), and poly (ethylene glycol)-poly(maleic anhydride-styrene) (A). (Front Ref. 42.)...

Fig. 1. Comparison of binding affinities of bovine serum albumin (BSA), polyvinylpyrrolidone (PVP), and polylysine (POLYLYS) for methyl orange anions (A), in acetate buffer, pH 5.6, 0.1 ionic strength, and 25°C.

Also remarkable in comparison with albumin is the very steep rise in binding with increasing concentration of methyl orange. In Fig. 4 this is most strikingly apparent in the smaller chain derivatives of the polymer... 

---