RENNIN

RENNIN Structure
CAS No.
9015-94-5
Chemical Name:
RENNIN
Synonyms
RENIN;RENNIN;RENNET;RENIN HUMAN;MUCORPEPSIN;EC 3.4.23.23;Native Human Renin;RENIN, HUMAN PLASMA;RENIN, HUMAN KIDNEY;RenninExCalfStomach
CBNumber:
CB3125788
Molecular Formula:
Molecular Weight:
0
MOL File:
Mol file
Modify Date:
2023/4/23 13:52:06

RENNIN Properties

storage temp. −20°C
form powder
color slightly brown
Merck 13,8218

SAFETY

Risk and Safety Statements

Hazard Codes  Xn
Risk Statements  36/37/38-42
Safety Statements  22-24-26-36/37
WGK Germany  1
3-10

RENNIN Chemical Properties,Uses,Production

Uses

Rennin is a milk coagulant that is an enzyme obtained from the abo- masum portion of the stomach of suckling mammals. it is most active at ph 3.8. one part purified rennin will coagulate more than five million parts of milk. the commercial extract of rennin is termed rennet. it is used to coagulate milk in making cheese, junket, and custard. see rennet.

Definition

An enzyme secreted by cellslining the stomach in mammals thatis responsible for clotting milk. Itacts on a soluble milk protein (caseinogen),which it converts to theinsoluble form casein. This ensuresthat milk remains in the stomachlong enough to be acted on by protein-digesting enzymes.

Biological Functions

Renin is an enzyme that is synthesized and stored in the renal juxtaglomerular apparatus and that catalyzes the formation of a decapeptide, angiotensin I, from a plasma protein substrate. Renin has a narrow substrate specificity that is limited to a single peptide bond in angiotensinogen, a precursor of angiotensin I. Renin is considered to control the rate-limiting step in the ultimate production of angiotensin II. Control of renin secretion by the juxtaglomerular apparatus is important in determining the plasma renin concentration.
Three generally accepted mechanisms are involved in the regulation of renin secretion. The first depends on renal afferent arterioles that act as stretch receptors or baroreceptors. Increased intravascular pressure and increased volume in the afferent arteriole inhibits the release of renin. The second mechanism is the result of changes in the amount of filtered sodium that reaches the macula densa of the distal tubule. Plasma renin activity correlates inversely with dietary sodium intake. The third renin secretory control mechanism is neurogenic and involves the dense sympathetic innervation of the juxtaglomerular cells in the afferent arteriole; renin release is increased following activation of 1-adrenoceptors by the neurotransmitter norepinephrine.
Angiotensin II, the primary end product of the renin–angiotensin system, acts on the juxtaglomerular cells to inhibit the release of renin; this process is therefore a negative feedback mechanism. The half-life of renin in the circulation is 10 to 30 minutes, with inactivation occurring primarily in the liver. Small amounts of renin are eliminated by the kidneys. Pure human renin has been used to develop specific inhibitors of the enzyme. Low-molecular-weight orally effective renin inhibitors are under development.

RENNIN Preparation Products And Raw materials

Raw materials

Preparation Products

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RENNIN RENIN RENNET RENIN HUMAN RENIN, HUMAN KIDNEY RENIN, HUMAN PLASMA MUCORPEPSIN Angiotensin forming enzyme EC 3.4.23.23 renin from hog kidney renin from porcine kidney RENIN, HUMAN RECOMBINANT RenninExCalfStomach Angiotensin forming enzyme, Renin from hog kidney RENIN FROM HOG KIDNEY, LYOPH., ~0.01 U/MG, 250 UG* Renin from Mouse, recombinant Renin from Human, Recombinant Native Human Renin Rabbit Anti-Renin antibody 9015-94-5 Proteolytic Enzymes and Substrates Selective Proteolytic Enzymes Enzymes, Inhibitors, and Substrates Biochemicals and Reagents BioChemical Renin-Angiotensin System ReninProteins and Derivatives Plasma&Blood Proteins Proteolytic Enzymes and Substrates Selective Proteolytic Enzymes