Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Seven strains of viridans streptococci of the species Streptococcus sanguis, S. mutans and S. mitis were investigated for autolysis. The effect of pH, salt concentration and temperature on the autolytic process was studied in Na2HPO4/NaH2PO4 buffer. Whole cells and walls of all strains autolysed most rapidly at pH values above 7. Autolysis of whole cells of S. sanguis and one strain of S. mitis (ATCC15909) was maximal in 0-05 TO 0-2 M buffer, while the two S. mutans strains and S. mitis ATCC15912 showed maximal autolysis in 0-5 and 1-0 M buffers. Cultures harvested in the stationary phase of growth possessed only slightly decreased autolytic activity compared with those from the exponential phase. Whole cells autolysed more rapidly at 37 degrees C Than at 45 degrees C and 10 degrees C. Autolysis of isolated walls of three strains of S. mitis (ATCC903, ATCC15909 and ATCC15912) was maximal at pH 7-0 AND 7-5 and in 1-0 M buffers. Streptococcus mitis ATCC15909 also showed maximal lysis in 0-01 M and 0-5 M buffers. An endopeptidase action of the autolytic system of S. mitis ATCC15912 was indicated by the progressive release of soluble amino groups during autolysis of the walls. No release of reducing groups was observed. Several free amino acids were released during autolysis of these walls, alanine, lysine and glutamic acid being in greatest quanitity.
J Gen Microbiol 1976 Sep
PMID:Autolysis in strains of viridans streptococci. 1 Mar 49

A neutral brain endopeptidase which hydrolyzes bradykinin (Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9) at the Phe5-Ser6 peptide bond was activated about 10 times by dithiothreitol. The preferential specificity of the enzyme for small peptides was suggested on the basis of the absence of activity toward a bradykinin-related protein such as S-carboxymethylated plasma kininogen.
Gen Pharmacol 1976 Aug
PMID:Rabbit brain thiol-activated endopeptidase. Hydrolysis of bradykinin and kininogen. 97 36

1. The effects of enkephalins and enkephalinase inhibitors were studied in CA1 area in rat hippocampal slices. 2. The data demonstrate a prevalent involvement of mu opiate receptors in the epileptogenic properties of enkephalins. 3. A potentiation of the mu opiate receptor-mediated epileptogenic response by enkephalinase inhibitors has been shown. 4. The results also show an inability to affect basal CA1 field potentials by inhibition of endogenous endopeptidase.
Gen Pharmacol 1991
PMID:An in vitro study on the hippocampal epileptogenic properties of enkephalins and enkephalinase inhibitors in rats. 165 89

Immunocytochemistry using polyclonal antisera raised to fragments or derivatives of locust adipokinetic hormone (AKH) I and IIs (Schooneveld et al., 1983, 1985, 1986) selectively stained cells in the nervous system of the free-living nematode, Panagrellus redivivus. Antiserum 528 (raised to the C-terminus of AKH IIs) stained the dorsal cephalic papillary cell bodies and the anterior nerve ring. Fibres in the lateral cords were stained with antiserum 241 that recognises the C-terminus of AKH I. Substances reacting to antisera 433 (raised to the N-terminal sequence of AKH I and IIs) 528 and 241 were present in the preanal ganglion and associated ventral nerve fibres. In males, all three antisera stained fibres leading to the base of the spicules. A peptide fraction from whole P. redivivus evoked an adipokinetic response in the locust, Schistocera gregaria which was dose dependent and was abolished by treatment with endopeptidase 24:11 but not by boiling or by incubation with leucine aminopeptidase. The adipokinetic activity was reduced by over 70% on incubation of the peptide fraction with pyroglutamyl aminopeptidase. The same fraction induced hyperglycaemia when injected into the cockroach, Periplaneta americana. These results are consistent with the existence in P. redivivus of peptides that are structurally related to the arthropod adipokinetic hormone/red pigment-concentrating hormone (AKH/RPCH) family.
Gen Comp Endocrinol 1991 Mar
PMID:The presence of peptides related to the adipokinetic hormone/red pigment-concentrating hormone family in the nematode, Panagrellus redivivus. 167 9

A cDNA copy of the M2 dsRNA encoding the K2 killer toxin of Saccharomyces cerevisiae was expressed in yeast using the yeast ADH1 promoter. This construct produced K2-specific killing and immunity functions. Efficient K2-specific killing was dependent on the action of the KEX2 endopeptidase and the KEX1 carboxypeptidase, while K2-specific immunity was independent of these proteases. Comparison of the K2 toxin sequence with that of the K1 toxin sequence shows that although they share a common processing pathway and are both encoded by cytoplasmic dsRNAs of similar basic structure, the two toxins are very different at the primary sequence level. Site-specific mutagenesis of the cDNA gene establishes that one of the two potential KEX2 cleavage sites is critical for toxin action but not for immunity. Immunity was reduced by an insertion of two amino acids in the hydrophobic amino-terminal region which left toxin activity intact, indicating an independence of toxin action and immunity.
Mol Gen Genet 1991 May
PMID:Expression in yeast of a cDNA copy of the K2 killer toxin gene. 204 53

Epstein-Barr virus (EBV)-positive Burkitt's lymphoma (BL) biopsy cells and early passage BL cell lines have been reported as showing an unusual type of virus-cell interaction; at least two EBV latent proteins appear not to be expressed. Serial passage of such lines is often accompanied by a broadening of virus latent gene expression and a corresponding change in the cell surface/growth phenotype towards that shown by in vitro transformed lymphoblastoid cell lines (LCLs). The sequence of events, both viral and cellular, involved in this transition needs to be defined properly. In the present work, phenotypically distinct cell clones have been derived from early passage cultures of a BL cell line in phenotypic transition, thereby giving access to relatively stable cell populations through which the different EBV-B cell interactions within the parental line can be studied. Clones retaining the original BL biopsy cell phenotype (CD10/CD77-positive, activation antigen/adhesion molecule-negative) expressed the virus-encoded nuclear antigen EBNA 1 but not any of the other known latent proteins, EBNAs 2, 3a, 3b, 3c, -LP and latent membrane protein (LMP). Other clones which had developed an LCL-like phenotype (CD10/CD77-negative, activation antigen/adhesion molecule-positive) now expressed all the above latent proteins and also contained significant numbers of cells in lytic cycle. Phenotypic change occurring within the parental BL cell line itself was initiated in a small subpopulation of cells in which the virus-encoded proteins EBNA 2 and LMP were transiently induced to an unusually high level of expression; this was accompanied by the first detectable changes in cell surface phenotype, namely the increase of cellular adhesion molecules. Some control over EBNA 2/LMP expression then appeared to be re-imposed since the presumed clonal descendents of these cells stably expressed EBNA 2 and LMP at much reduced levels typical of those seen in conventional LCLs.
J Gen Virol 1990 Jul
PMID:Different Epstein-Barr virus-B cell interactions in phenotypically distinct clones of a Burkitt's lymphoma cell line. 216 33

The pattern and kinetics of degradation of native salmon gonadotropin-releasing hormone (sGnRH) and mammalian leuteinizing hormone-releasing hormone (LHRH) by pituitary bound enzymes were studied in the gilthead seabream, Sparus aurata. sGnRH and LHRH were incubated for different periods of time with membrane or cytosolic fractions of pituitary homogenates. At the end of the incubation, the degradation mixture was fractionated on reverse-phase high-pressure liquid chromatography. The degradation products were identified by comparing their retention times to those of synthesized GnRH fragments and by analyzing their amino acid composition. The main GnRH degradative activity resides in the cytosolic fraction of the pituitary homogenate. Both sGnRH and LHRH are rapidly degraded by pituitary cytosol, with 78.3 and 87.7% of the peptides, respectively, cleaved after 3 hr of incubation. Maximal degradation of sGnRH occurred at a pH range of 7 to 8. The main initial products of degradation of sGnRH and LHRH are the 1-5, 6-10, and 1-9 fragments. This suggests the involvement of two site-specific peptidases, a Tyr5-Gly6 endopeptidase and a Pro9-Gly10NH2 peptidase or postproline cleaving enzyme. While the 1-6 and 1-9 fragments undergo rapid secondary degradation, the 1-5 is relatively stable. Competition experiments suggest that the endopeptidase cleaving the sGnRH at the Tyr5-Gly6 bond is not specific to the neuropeptide and is probably a general proteolitic enzyme. However, the cleavage at the 9-10 bond has a high degree of specificity to the Pro9-Gly10NH2 sequence found in sGnRH. The two proposed pituitary peptidases of S. aurata have some characteristics similar to those of rat hypophyseal and hypothalamic GnRH cleaving enzymes. No differences are found in hypophyseal GnRH degradative activity between females with occytes undergoing previtellogenesis or advanced stages of vitellogenesis.
Gen Comp Endocrinol 1990 Aug
PMID:Degradation of gonadotropin-releasing hormones in the gilthead seabream, Sparus aurata. I. Cleavage of native salmon GnRH and mammalian LHRH in the pituitary. 220 10

The pattern and kinetics of degradation of native salmon gonadotropin-releasing hormone (sGnRH), mammalian luteinizing hormone-releasing hormone (LHRH), and some of their analogs by cytosolic enzymes of pituitary, kidney, and liver were studied in the gilthead seabream, Sparus aurata. The native peptides sGnRH and LHRH are rapidly degraded by all three tissues, LHRH being degraded faster than sGnRH. The kinetics of production of the peptide fragments suggest that initial cleavage of sGnRH and LHRH in the three studied tissues occurs at the 5-6 and 9-10 bonds. This indicates the initial activity of a Tyr5-Gly6 endopeptidase and a Pro9-Gly10NH2 peptidase or postproline cleaving enzyme. Secondary degradation of the main initial fragments (1-5, 6-10, and 1-9) is more intensive in the kidney than in the pituitary or liver. Substitution of the position 6 amino acid glycine by a dextrorotatory (D) amino acid such as in the D-Trp6-LHRH renders the 5-6 bond resistant to cleavage. However, whereas [D-Trp6]-LHRH is intensively cleaved at the Pro9-Gly10NH2 bond by the pituitary, its cleavage at this site by the kidney and liver is slow. This suggests a low activity of the Pro9-Gly10NH2 peptidase in the kidney and liver as compared to the pituitary. When, in addition to the position 6 substitution, the carboxy terminus Pro9-Gly10NH2 is modified to Pro9NET, such as in the [D-Ala6-Pro9NET]-LHRH and the [D-Arg6-Pro9NET]-sGnRH, the 9-10 cleavage site is also blocked, resulting in GnRH analogs highly resistant to degradation. The relationships between susceptibility of the different forms of GnRH to enzymatic degradation by the pituitary, kidney, and liver and their relative biological activities in S. aurata are discussed. We conclude that increased resistance of GnRH analogs to enzymatic degradation contributes to their superactivity.
Gen Comp Endocrinol 1990 Aug
PMID:Degradation of gonadotropin-releasing hormones in the gilthead seabream, Sparus aurata. II. Cleavage of native salmon GnRH, mammalian LHRH, and their analogs in the pituitary, kidney, and liver. 220 11

In Bacillus subtilis the alpha, beta, gamma and delta components comprise 80-90% of the total acid-soluble spore proteins (ASSPs). Sequence analysis demonstrates that alpha and beta share 32 of their first 36 amino acids and are closely related to the A and C ASSPs of Bacillus megaterium spores, confirming the results of analysis of their cloned genes. Despite the difference in apparent size of gamma and delta, they have identical N-terminal sequences (37 residues). Unless gamma and delta derive from very recently duplicated genes, it appears that gamma is derived from delta, either in vivo or during isolation. Although the sequenced regions of gamma and delta have no homology to alpha and beta, outside of the previously recognized pentapeptide recognition sequence for the spore endopeptidase, they share 10 and 15 residue peptides flanking this sequence with ASSP B of B. megaterium, but in reverse order. At least two groups of ASSPs have, therefore, been conserved between B. subtilis and B. megaterium: the multigene AC alpha beta family and the B gamma (delta) group. Sequence conservation in each group implies selection for functions in addition to storage. Both the alpha and beta components of B. subtilis ASSPs and their mRNAs are located in the forespore compartment of cells at t5.5 of sporulation, the time of most rapid ASSP synthesis. The sizes of these transcripts (250-350 bp) and their ability to direct the in vitro synthesis of ASSPs of mature size, indicate that genes for these ASSPs are monocistronic, consistent with dispersed map location. Synthesis of ASSPs is, therefore, coordinately controlled by selective transcription in the forespore.
J Gen Microbiol 1987 Aug
PMID:The major acid-soluble proteins of Bacillus subtilis spores: partial amino acid sequence and forespore location of their mRNAs. 245 Sep 63

Melanin concentrating hormone (MCH) is a heptadecapeptide isolated from chum salmon (Oncorhynchus keta) pituitaries. The peptide has been isolated from whole brain extract at a low yield of 1.2 micrograms/1300 brains. MCH activity in the hypothalamus was characterised by in vitro scale bioassay and radioimmunoassay. Specificity of these assay systems was examined with neurotransmitters such as epinephrine, norepinephrine, and dopamine, hypothalamic hormones such as somatostatin, isotocin, Arg-vasotocin, oxytocin, and Arg-vasopressin, and salmon prolactin and its chymotryptic peptide or salmon PRL176-187. Among them only salmon PRL176-187 exhibited weak activities in both assays. The neurotransmitters were 10(4) to 10(5) times less potent than MCH in the bioassay. MCH concentrations in a pituitary and a hypothalamus were estimated as 5300 +/- 750 ng (ca. 106 micrograms/g) and 48 +/- 9.5 ng (ca. 1.6 micrograms/g), respectively, by radioimmunoassay. Lysyl endopeptidase digestion of the hypothalamic extract resulted in a significant increase of biological activity as well as of immunoreactivity. Gel filtration of the hypothalamic extract and subsequent enzymatic digestion revealed that the fractions at higher molecular weight were contributory to the increase in the activities.
Gen Comp Endocrinol 1987 Mar
PMID:Characterization of melanin concentrating hormone in teleost hypothalamus. 288 42


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