Alpha, Beta, Gamma, Omega—The Structure of the Plasma Proteins

Maximizing recombinant human serum albumin production in a MutsPichia pastoris strain

“…Approximately 35–40 g of HSA is present in a liter of blood. HSA not only maintains normal osmolality in the blood stream but also transports a variety of small molecules such as vitamins, hormones, fatty acids, amino acids, metabolites, drugs, and divalent metal ions like Zn, Cu, and Co . HSA is also a source of reserve protein in conditions like hypoproteinemia where the blood has abnormally low levels of protein.…”

Inhibition of rennets by blood serum

“…α 2 ‐Macroglobulin has a very broad specificity and inhibits the four classes of proteinases: serine, metallo, cysteine and aspartate (Barrett and Starkey 1973; Hiroyasu 1973; Makoto et al. 1974; Putnam 1984). α 2 ‐Macroglobulin has a unique mechanism of proteinase inhibition: the proteinase binds to the inhibitor and cleaves a specific peptide bond in the ‘bait’ region of the α 2 ‐M molecule and induces a conformational change in the α 2 ‐M, as a result of which the proteinase molecule is entrapped and inhibited within the modified α 2 ‐M molecule (Barrett and Starkey 1973).…”

“…small increase in the RCT of milk coagulated with methylamine-treated calf chymosin indicated that the methylamine inhibited calf chymosin only slightly, probably because of an increase in pH caused by the buffer (pH 7.5) in which methylamine was dissolved. The evidence from literature that a 2 -M is the rennet-inhibitor in blood serum and the fact that methylamine-treated serum failed to inhibit the activity of calf chymosin strongly suggest that the principal rennet-inhibitor in blood serum is a 2 -M. a 2 -Macroglobulin has a very broad specificity and inhibits the four classes of proteinases: serine, metallo, cysteine and aspartate (Barrett and Starkey 1973;Hiroyasu 1973;Makoto et al 1974;Putnam 1984). a 2 -Macroglobulin has a unique mechanism of proteinase inhibition: the proteinase binds to the inhibitor and cleaves a specific peptide bond in the 'bait' region of the a 2 -M molecule and induces a conformational change in the a 2 -M, as a result of which the proteinase molecule is entrapped and inhibited within the modified a 2 -M molecule (Barrett and Starkey 1973).…”

Ceruloplasmin, transferrin and apolipoprotein A-II play important role in treatment's follow-up of paracoccidioidomycosis patients

“…These proteins, as well as tissue molecules, can be used for diagnosing and monitoring the therapy [ 34 ]. Although 1,175 proteins have been described in human plasma [ 35 ], only 10 of them constitute 95% of the total protein content [ 36 , 37 ]: albumin (54%), immunoglobulin G (17%), alpha-1-antitrypsin (3.8%), alpha-2-macroglobulin (3.6%), immunoglobulin A (3.5%), transferrin (3.3%), haptoglobin (3%), apolipoprotein A-1 (3%), immunoglobulin M (2%) and alpha-1 acid glycoprotein (1.3%).…”