C-peptide does not affect the blood sugar level in the body.

A person with type 2 diabetes has a normal or high level of C-peptide.

A person with an insulinoma will have a high level of C-peptide in the blood.

The level of C-peptide in the blood can show how much insulin is being made by the pancreas.

This should decrease the amount of insulin and C-peptide that the body releases into the blood.

Laboratory tests measure substances in the blood, such as glucose, insulin, and C-peptide.

Though not yet commercially available, C-peptide has shown promising results in treatment of diabetic complications, including neuropathies.

C-peptide, which is secreted into the bloodstream in equimolar quantities to insulin.

C-peptide, a by-product of insulin production, may provide new hope for patients suffering from diabetic nephropathy.

A person whose pancreas does not make any insulin (type 1 diabetes) has a low level of insulin and C-peptide.

Mature insulin has 39 fewer amino acids; 4 are removed altogether, and the remaining 35 form the C-peptide.

The C-peptide of proinsulin (discussed later), however, differs much more among species; it is also a hormone, but a secondary one.

C-peptide also has been reported to have anti-inflammatory effects as well as aid repair of smooth muscle cells.

This test measures residual beta cell function by determining the level of insulin secretion (C-peptide).

C-peptide helps to prevent neuropathy and other vascular deterioration related symptoms of diabetes mellitus.

Proinsulin C-peptide was first described in 1967 in connection with the discovery of the insulin biosynthesis pathway.

Finally, proinsulin is converted into the bioactive hormone insulin by removal of its connecting peptide (C-peptide).

Then the C-peptide is removed, leaving the A-chain and B-chain that constitute the insulin molecule.

Thus, IPCs respond to glucose challenge in vivo by releasing insulin C-peptide.

During the past decade, however, C-peptide has been found to be a bioactive peptide in its own right, with effects on microvascular blood flow and tissue health.

When the beta cell produces insulin from proinsulin, a connecting peptide (or C-peptide) is also manufactured and released into the bloodstream.

In 1983, he won the State Invention Second Prize for his new achievement in synthesis of the C-peptide.

Absence of C-peptide in the blood indicates that insulin has not been released from the pancreas, and this fact confirms the diagnosis of diabetes type 1.

Persons with LADA typically have low, although sometimes moderate, levels of C-peptide as the disease progresses.

The expressed protein contains two conserved domains, a C-peptide (or aristaless domain) and the prd-like class homeobox domain.

C-peptide does not affect the blood sugar level in the body.

A person with type 2 diabetes has a normal or high level of C-peptide.

A person with an insulinoma will have a high level of C-peptide in the blood.

The level of C-peptide in the blood can show how much insulin is being made by the pancreas.

This should decrease the amount of insulin and C-peptide that the body releases into the blood.

Laboratory tests measure substances in the blood, such as glucose, insulin, and C-peptide.

Though not yet commercially available, C-peptide has shown promising results in treatment of diabetic complications, including neuropathies.

C-peptide, which is secreted into the bloodstream in equimolar quantities to insulin.

C-peptide, a by-product of insulin production, may provide new hope for patients suffering from diabetic nephropathy.

A person whose pancreas does not make any insulin (type 1 diabetes) has a low level of insulin and C-peptide.

Mature insulin has 39 fewer amino acids; 4 are removed altogether, and the remaining 35 form the C-peptide.

The C-peptide of proinsulin (discussed later), however, differs much more among species; it is also a hormone, but a secondary one.

C-peptide also has been reported to have anti-inflammatory effects as well as aid repair of smooth muscle cells.

This test measures residual beta cell function by determining the level of insulin secretion (C-peptide).

C-peptide helps to prevent neuropathy and other vascular deterioration related symptoms of diabetes mellitus.

Proinsulin C-peptide was first described in 1967 in connection with the discovery of the insulin biosynthesis pathway.

Finally, proinsulin is converted into the bioactive hormone insulin by removal of its connecting peptide (C-peptide).

Then the C-peptide is removed, leaving the A-chain and B-chain that constitute the insulin molecule.

Thus, IPCs respond to glucose challenge in vivo by releasing insulin C-peptide.

During the past decade, however, C-peptide has been found to be a bioactive peptide in its own right, with effects on microvascular blood flow and tissue health.

When the beta cell produces insulin from proinsulin, a connecting peptide (or C-peptide) is also manufactured and released into the bloodstream.

In 1983, he won the State Invention Second Prize for his new achievement in synthesis of the C-peptide.

Absence of C-peptide in the blood indicates that insulin has not been released from the pancreas, and this fact confirms the diagnosis of diabetes type 1.

Persons with LADA typically have low, although sometimes moderate, levels of C-peptide as the disease progresses.

The expressed protein contains two conserved domains, a C-peptide (or aristaless domain) and the prd-like class homeobox domain.

Finally, proinsulin is converted into the bioactive hormone insulin by removal of its connecting peptide (C-peptide).

Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions.

When the beta cell produces insulin from proinsulin, a connecting peptide (or C-peptide) is also manufactured and released into the bloodstream.

Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions.

C-peptide is the abbreviation for "connecting peptide", although its name was probably also inspired by the fact that insulin is also composed of an "A" chain and a "B" chain.

Structurally, beta and gamma crystallins are composed of two similar domains which, in turn, are each composed of two similar motifs with the two domains connected by a short connecting peptide.