Fragments from Human Serum Albumin

Immunochemistry of Fragments from Human Serum Albumin 

Several immunochemically reactive fragments were isolated fi om HSA by chymotryptic hydrolysis (Press and Porter, 1962), by tryptic 

Trypsin hydrolyzed HSA less efficiently (pH 8, 37 C, 24 hr), yielding a mixture of fragments of molecular weights 12,000-30,000 (Lapresle et al., 1959). These fragments gave 65% precipitation with anti-HSA relative to HSA. The mixture was not fractionated, and no peptides possessing inhibitory activity toward HSA-anti-HSA were reported. 

Structural and Inununochemical Studies on Serum Albumin from Various Species 

---

B. Immunochemistry of Fragments from Human Serum Albumin... 

Serum albumin, the most abundant plasma protein, has been subjected to extensive studies which resulted in a wealth of information on its chemical and physicochemical properties. Only recently has the amino acid sequence of bovine and human serum albumins become known. Prior to the availability of the amino acid sequence, immunochemical studies on BSA or HSA were hampered by the inability to assign an immunochemically reactive fragment within the sequence of the albumin molecule. With the availability of the sequence, it is becoming possible to identify immunochemically reactive fragments of known sequences. Thus fragments 11-193 and 377-571 were isolated from BSA. These fragments were shown to have rather unusual immunochemical properties. Each... 

Labeling of human serum albumin (H S A) was carried out by acylation of a fraction of its lysines with the N-succinimidyl ester of the complex [Re(bcp)(CO)3-(4-COOHPy)]Cl04 where bcp is 2,9-dimethyl-4,7-diphenyl-l,10-phenantroline, and 4-COOHPy is isonicotinic acid. This ester Re-L48, is synthesized in 3 steps starting from bcp, as shown in Scheme 8.20. It is then coupled to HSA to give the complex (Re-L) -HSA [56]. On average, two Re(CO)3 fragments per molecule of HSA are conjugated. 

---