B chain

The molecular weight of the B chain is approximately 76.5kDa.

Many plants such as barley have the A chain but not the B chain.

After their marriage they amalgamated the two operations, and formed the F and B chain.

This activity was observed over fifty years ago, though the enzyme specifically responsible for B chain cleavage was identified more recently.

IDE was first identified by its ability to degrade the B chain of the hormone insulin.

Meizothrombin contains fragment 1-2 A chain linked to the B chain by a disulfide bond.

Franz H: Mistletoe lectins and their A and B chains.

Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue.

Cleavage of Ala-Leu and Tyr-Leu in B chain of insulin.

Preferential cleavage of Gly-Ser in B chain of insulin most rapidly, followed by Leu!

The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid.

It is understood that IDE cleaves insulin B chain as well as amyloid β at several sites.

Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene.

Insulin glargine have substitution of glycine for asparagine at A21 and two arginines added to the carboxy terminal of B chain.

The B chain contains two intramolecular disulfide bonds and is connected to the A chain through two intermolecular disulfide bridges.

The two chains formed after the cleavage at Arg, termed the A and B chains, are linked by a disulfide bond in active thrombin.

The C-peptide is abstracted from the center of the proinsulin sequence; the two other ends (the B chain and A chain) remain connected by disulfide bonds.

It has two noncovalently associated polypeptide chains: an A chain sequence with 44 amino acid residues, and a B chain with 50 residues.

People do not get sick from eating large amounts of such products, as ricin A is of extremely low toxicity as long as the B chain is not present.

These toxins consist of an AB5 multimer structure, in which a pentamer of B chains has a membrane-binding function and an A chain is needed for enzymatic activity.

Insulin Turbidity Assay: PDI breaks the two disulfide bonds between two insulin (a and b) chains that results in precipitation of b chain.

Ricin toxin A chain and ricin toxin B chain are of similar molecular weights, approximately 32 kDa and 34 kDa, respectively.

Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu-Tyr, Tyr-Leu and Phe-Phe of insulin B chain.

Subsequent cleavage of meizothrombin by Factor Xa at Arg gives Fragment 1-2 and active thrombin, consisting of the A and B chains linked by a disulfide bond.

Finally, because the A and B chains are physiologically inactive without the three linking disulfide bonds (two interchain, one intrachain on A), Sanger and coworkers determined their assignments in 1955.