BSA

Hydroxylysine (328) was synthesized by chemoselective reaction of (Z)-4-acet-oxy-2-butenyl methyl carbonate (325) with two different nucleophiles first with At,(9-Boc-protected hydroxylamine (326) under neutral conditions and then with methyl (diphenylmethyleneamino)acetate (327) in the presence of BSA[202]. The primary allylic amine 331 is prepared by the highly selective monoallylation of 4,4 -dimethoxybenzhydrylamine (329). Deprotection of the allylated secondary amine 330 with 80% formic acid affords the primary ally-lamine 331. The reaction was applied to the total synthesis of gabaculine 332(203]. 

Bryamycin Bryostatin 1 BSA-SILICA B-stage B-stage resins B. subtilis 66333 BTEPE [37853-59-1]... 

The available free carboxyl groups of the DAS—HMS can be linked via a peptide bond to available primary amine groups onto highly antigenic carriers using a carbodiimide (19). The carriers used in this case were bovine semm albumin (BSA) and poly-L-lysine (molecular weight 150,000 to 300,000). The... 

Protection of carboxyflc acids and sulfenic acids requires efficient sdyl donors, eg, BSA, MTSA, and bis(ttimeth5isdyl)urea [18297-63-7] (BSU). BSU is often prepared in situ from hexamethyldisda2ane and urea to yield over 90% of the sdylated derivative in synthesis of cephalosporins (5). 

Fig. 3. Synthesis of diacidic and monoacidic N-1 a2etidinone phosphonates and phosphinates where TMSBr is trimethylsilyl bromide BSA is...

The first observation of the enantioselective properties of an albumin was made in 1958 (28) when it was discovered that the affinity for L-tryptophan exceeded that of the D-enantiomer by a factor of approximately 100. This led to more studies in 1973 of the separation of DL-tryptophan [54-12-6] C22H22N2O2, on BSA immobilized to Sepharose (29). After extensive investigation of the chromatographic behavior of numerous racemic compounds under different mobile-phase conditions, a BSA-SILICA hplc column (Resolvosil-R-BSA, Macherey-Nagel GmvH, Duren, Germany) was... 

Retention and stereoselectivity on the BSA columns can be changed by the use of additives to the aqueous mobile phase (30). Hydrophobic compounds generally are highly retained on the BSA, and a mobile-phase modifier such as 1-propanol can be added to obtain reasonable retention times. The retention and optical resolution of charged solutes such as carboxyUc acids or amines can be controlled by pH and ionic strength of the mobile phase. 

Appllca.tlons. Various A/-derivatives of amino acids (qv) are resolvable on BSA columns. These /V-amino acid derivatives include ben2enesulfonyl-, phthalimido-, S-dimethylarnino-l-naphthalenesulfonyl- (DANSYL-), 2,4-dinitrophenyl- (DNP-), and 2,3,6-trinitrophenyl- (TNP-) derivatives (30). Amines such as Prilocain, ( )-2-(prop5lamino)-(9-propiono-toluidide, a local anesthetic (Astra Pharm. Co.), are also resolved on BSA. The aromatic amino acids DL-tryptophan, 5-hydroxy-DL-tryptophan, DL-kynurenine [343-65-7] C qH 2N 2 3 3-hydroxy-DT.-kynurenine [484-78-6] and dmgs... 

Approved techniques for manual and mechanical sampling are often documented for various commodities handled in commerce by industiy groups. Examples are the International Standards Organization (ISO), British Standards Association (BSA), Japan Institute of Standards (JIS), American Society for Testing Materi s (ASTM), and the Fertihzer Institute. Sampling standards developed for use in specified industry applications frequently include instructions for labora-toiy work in sample preparation and analysis—steps (2) and (3) above. 

Three different types of columns packed with gels of different pore sizes are available. Columns should be selected that are suitable for the molecular weight range of specific samples, as each type has a different exclusion limit (Fig. 6.41, page 215). Bovine serum albumin (BSA), myoglobin, and lysozyme show good peak shapes using only 100 mM of sodium phosphate buffer as an eluent. There is no need to add any salt to the eluent to reduce the ionic interaction between protein and gel. 

FIGURE 7.2 (A) Separation of a standard protein mixture. A test mixture consisting of BSA... 

FIGURE 7.4 Separation of a standard protein mixture on a Fractogel EMD BioSEC-column (600-16 mm) after incubation with 30% acetonitrile. The sample contained BSA ( ), ovalbumin ( ), and cytochrome c (A) (sample volume 500 ftl flow rate 1.0 ml/min). No significant shifts of the retention times and no loss of the resolution were observed even after 900 hr of exposure. 

FIGURE 7.6 Effect of column length on the separation efficiency. Two different Fractogel EMD BioSEC columns (A 600 X 16 mm, B 1000 X 16 mm) were tested using BSA, ovalbumin, and cytochrome c (S/S/3 mg/ml) as sample (20 m/VI sodium dihydrogen phosphate, 300 m/VI NaCI, pH 7.2 0.5 ml/min). Better resolution can be achieved using longer columns. 

---