Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

gamma-Thrombin was produced during autolysis or limited proteolysis of coagulant gamma-thrombin. This thrombin form loses its ability to coagulate fibrinogen but preserves the esterase and amidase activity on the low-molecular-weight synthetic substrates. This evidences for the integrity of the active site of gamma-thrombin and for the integrity break of the enzyme molecule region responsible for the binding with fibrinogen. gamma-Thrombin with the minimal coagulating activity, possessing high esterase and amidase activity is obtained. Fibrin-agarose possessing affinity to gamma-thrombin and specifically not binding gamma-thrombin was used to remove admixtures of the coagulant gamma-thrombin from the preparations of gamma-thrombin obtained during the enzyme autolysis.
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PMID:[Affinity chromatography of human gamma-thrombin on fibrin-agarose]. 318 51

Human alpha-thrombin was poorly immunogenic in Balb/c mice. Nevertheless, following fusion of spleen cells from a responding mouse with NS-1 cells, 8 mouse monoclonal antibodies against alpha-thrombin were isolated, and 6 were characterised. Five of these were isotype IgG2a, and one was IgG1. One, EST 1, bound thrombin only minimally, and was directed against a neoantigen on the thrombin-ATIII (T-AT) complex. This antibody also recognised a site on prothrombin, though with much lower affinity. Its binding was markedly temperature-dependent, indicating a requirement for molecular mobility. A second antibody, EST 4, would not bind the T-AT complex. It inhibited both the clotting and amidase activities of thrombin, and modification of the active site histidine, but not the active site serine, reduced the affinity constant of binding to EST 4. This antibody appears to be directed against an epitope in the vicinity of the enzyme active site. The epitopes for EST 1 and EST 4 were both remote from those of the other monoclonal antibodies, EST 2, 6, 7 and 8. These four competed with each other for binding to thrombin, and all inhibited clotting but not amidase activity. Thrombin binding was not affected by modification of the active site, though formation of the T-AT complex reduced the affinity of binding to EST 6 and EST 8. These monoclonals recognise epitopes in the region of the fibrinogen binding site.
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PMID:Monoclonal antibodies directed against human alpha-thrombin and the thrombin-antithrombin III complex. 652 47

Salivary gland products of haematophogous insects including tsetse flies (Diptera: Glossinidia) are involved in antihaemostasis to allow for efficient blood feeding. In addition, salivary products of tsetse are thought to indirectly support the metacyclogenesis and eventual transmission of the African trypanosome protozoan parasites to their mammalian hosts. We have previously characterized the major anticoagulant, Tsetse Thrombin Inhibitor (TTI), from salivary extracts, and described molecular aspects of its cDNA from a Glossina morsitans morsitans salivary gland cDNA library. In addition, a family of two related genes with growth factor and adenosine-deaminase motifs (TSGF-1 and TSGF-2) have also been described. Here, we report on the molecular aspects of three different cDNAs and their putative products expressed in salivary glands: cDNAs TAg5, Tsal1 and Tsal2. The full-length transcript encoded by Tsetse Antigen 5 (TAg5) cDNA is 926 bp excluding the poly(A) stretch, and has an open reading frame of 259 amino acids that can encode for a protein of 28 925 Da. The putative product of TAg5 shows extensive similarities to cDNAs characterized from Drosophila (Agr and Agr2) and sandfly Lutzomyia (LuLoAG5). The cDNAs Tsal1 and Tsal2 are predicted to encode for mature proteins of 45 612 Da (399 amino acids) and 43 930 Da (389 amino acids), respectively, and their putative products exhibit over 42% identity to one another. The N terminus of each putative protein contains a hydrophobic region with signal peptide characteristics indicating that they may be secretory in nature. Transcripts specific for TAg5 and Tsal2 genes can be detected in all developmental stages of tsetse while Tsal1 expression is limited to adult and larval stages. A reverse transcription polymerase chain reaction based amplification approach indicates that TAg5 transcipts can be detected from proventriculus and midgut tissues of the fly in addition to salivary glands, while Tsal1 and Tsal2 expression is restricted to salivary gland and proventriculus. The salivary glands of adult males are found to express higher levels of TAg5 and Tsal2 in comparison to females while no significant sex-based difference is observed for Tsal1 expression. The expression of these cDNAs in different tsetse species (G. m. morsitans, Glossina austeni and Glossina fuscipes) shows wide variations.
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PMID:Characterization of genes expressed in the salivary glands of the tsetse fly, Glossina morsitans morsitans. 1124 Jun 38