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INSULIN 구조식 이미지
카스 번호:
ProMaxx;INSULIN;27USP U/MG;insulin(ox);Insulin beef;bovineinsulin;INSULIN BOVINE;Insulin (cattle);Insulinfrombovine;insulin bovine usp
포뮬러 무게:
MOL 파일:
Mol file


저장 조건
acidified water, pH 2.0: 2 mg/mL
물리적 상태
Stable. Incompatible with strong oxidizing agents. Keep refrigerated at -20 C
CAS 데이터베이스


안전지침서 22-24/25
WGK 독일 3
RTECS 번호 NM8900250
F 고인화성물질 3-10

INSULIN C화학적 특성, 용도, 생산

화학적 성질

white solid

화학적 성질

Insulin is a relatively simple protein consisting of 51 amino acids arranged as two polypeptide chains, an α- chain and β-chain, connected by disulfide bonds; the latter are necessary to maintain tertiary structure and biological activity. Although the amino acid sequence and composition of animal insulins may differ slightly from those of human insulin, their biological actions are similar. Alteration of specific amino acid residues within the insulin molecule yields novel derivatives that vary in their pharmacokinetics and binding affinity for the insulin receptor. Some insulin analogues display mitogenic properties in addition to their metabolic effects.




A polypeptide hormone having a molecular weight of 5733. It is formed in the islets of Langerhans located in the pancreas and was so named for this reason. Insulin is composed of 16 amino acids arranged in a coiled chain and crosslinked in several places


More than a century has passed since von Mering and Minkowski first demonstrated that pancreatectomized dogs exhibited signs and symptoms characteristic of diabetes mellitus. Shortly thereafter, Banting and Best used pancreatic extracts to reverse these symptoms in diabetic patients, thus providing a basis for establishing a cause-and-effect relationship between insulin deficiency and diabetes. Insulin was subsequently isolated, crystallized, and eventually synthesized in the laboratory. Insulin replacement therapy has been widely used in the clinical management of diabetes mellitus for more than 70 years. In 1982, recombinant DNA (rDNA) derived human insulin was first produced and is now widely used instead of insulin derived from beef or pork. More recently, insulin analogues have been produced that modulate the activity and rate of insulin action.


Overdosage can be fatal.


Insulin is usually administered subcutaneously. Depending on the type of insulin being administered, the rate of insulin absorption can be modulated by altering the polymerization of the insulin molecule (e.g., monomers, dimers, or hexamers). Intramuscular injections of insulin are used less often because absorption is more rapid. Being a polypeptide hormone, insulin is readily inactivated if administered orally. In emergencies, such as severe diabetic ketoacidosis, insulin can be given intravenously. Clinical studies are examining the efficacy and safety of inhaled insulin, which may be promising for some patients.
Once insulin enters the circulation, its plasma halflife is less than 10 minutes. Hepatic insulinases destroy approximately 50% of circulating insulin, with the remainder degraded by circulating proteases. Therefore, only a relatively small amount of the total endogenous insulin secreted ever reaches the peripheral tissues. Although a number of tissues accumulate small amounts of insulin, the liver and kidney are the principal sites of hormone uptake and degradation. Insulin metabolism is accomplished both through the actions of an insulinspecific protease found in the cytosol of many tissues and by the reductive cleavage of the insulin disulfide bonds by glutathione–insulin transhydrogenase. In the kidney, insulin that undergoes glomerular filtration is almost completely reabsorbed and metabolized within the proximal convoluted tubules of the nephron.

INSULIN 준비 용품 및 원자재


준비 용품


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