Biomaterial Database

The kallikrein, kininase and related peptides activities in central Asian snake venoms. 1992

Yukelson LYa, and V M L'vov, and A V Shkinev, and N Sultanalieva

Institute of Biochemistry, Uzbek Academy of Sciences, Tashkent, Republic Uzbekistan.

The quantitative content estimation of kininogenases, kininases and related peptides have been made for Central Asian snake venoms: V. lebetina turanica and E. multisquamatus (gen. Vipera and Echis, fam. Viperidae), Ag. halys halys (gen. Agkistrodon, fam. Crotalidae) and N. oxiana (gen. Naja, fam Elapidae). It has been demonstrated, that all venoms investigated cause the contractile effect, when acting on isolated smooth muscle preparations. Kinin-like contractile activity was found in the low molecular weight fraction of the cobra venom. This action has the prolonged character as compared with bradykinin, but apart from it, results in the inactivation of the rat uterus because of cytotoxic components presence. The specific bradykinin-potentiating effect of the low molecular weight fraction of the E. multisquamatus venom has been discovered. It has been found, that the effect is connected with inhibition of the kininase II (angiotensin I converting enzyme, ACE). Two peptide inhibitors was isolated and characterized from this fraction.

UI	MeSH Term	Description	Entries
D007610	Kallikreins	Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).	Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D007703	Peptidyl-Dipeptidase A	A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide-\|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of ANGIOTENSIN I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no action on angiotensin II. It is also able to inactivate BRADYKININ, a potent vasodilator; and has a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. (From https://www.uniprot.org April 15, 2020).	ACE1 Angiotensin-Converting Enzyme 1,ACE1 Protein,Angiotensin Converting Enzyme,Angiotensin Converting Enzyme 1,Antigens, CD143,CD143 Antigens,Dipeptidyl Carboxypeptidase I,Kininase II,Peptidase P,Angiotensin I-Converting Enzyme,Carboxycathepsin,Dipeptidyl Peptidase A,Kininase A,ACE1 Angiotensin Converting Enzyme 1,Angiotensin I Converting Enzyme,Carboxypeptidase I, Dipeptidyl,Peptidyl Dipeptidase A
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009119	Muscle Contraction	A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.	Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D003435	Crotalid Venoms	Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.	Bothrops Venom,Crotalidae Venoms,Pit Viper Venoms,Rattlesnake Venoms,Crotactin,Crotalid Venom,Crotalin,Crotaline Snake Venom,Crotalotoxin,Crotamin,Pit Viper Venom,Rattlesnake Venom,Snake Venom, Crotaline,Venom, Bothrops,Venom, Crotalid,Venom, Crotaline Snake,Venom, Pit Viper,Venom, Rattlesnake,Venoms, Crotalid,Venoms, Crotalidae,Venoms, Pit Viper,Venoms, Rattlesnake,Viper Venom, Pit
D004546	Elapid Venoms	Venoms from snakes of the family Elapidae, including cobras, kraits, mambas, coral, tiger, and Australian snakes. The venoms contain polypeptide toxins of various kinds, cytolytic, hemolytic, and neurotoxic factors, but fewer enzymes than viper or crotalid venoms. Many of the toxins have been characterized.	Cobra Venoms,Elapidae Venom,Elapidae Venoms,Naja Venoms,Cobra Venom,Elapid Venom,Hydrophid Venom,Hydrophid Venoms,King Cobra Venom,Naja Venom,Ophiophagus hannah Venom,Sea Snake Venom,Sea Snake Venoms,Venom, Cobra,Venom, Elapid,Venom, Elapidae,Venom, Hydrophid,Venom, King Cobra,Venom, Naja,Venom, Ophiophagus hannah,Venom, Sea Snake,Venoms, Cobra,Venoms, Elapid,Venoms, Elapidae,Venoms, Hydrophid,Venoms, Naja,Venoms, Sea Snake
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D012910	Snake Venoms	Solutions or mixtures of toxic and nontoxic substances elaborated by snake (Ophidia) salivary glands (Duvernoy's gland) for the purpose of killing prey or disabling predators and delivered by grooved or hollow fangs. They usually contain enzymes, toxins, and other factors.	Duvernoy's Gland Secretion,Duvernoy's Secretion,Snake Toxin,Snake Toxins,Snake Venom,Duvernoy Gland Secretion,Duvernoy Secretion,Duvernoys Gland Secretion,Duvernoys Secretion,Secretion, Duvernoy's,Secretion, Duvernoy's Gland,Toxin, Snake,Venom, Snake