Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.27 (thermolysin)
 1,894 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A laser-induced luminescence technique is introduced for probing the structure and equilibria of lanthanide complexes and lanthanide ion binding to macromolecules. The method involves the excitation of the 7F0 leads to 5D0 transition between nondegenerate levels in the europium(III) ion by means of an intense pulsed dye laser source. Excitation profits obtained by scanning the laser through the transition region reveal distinct peaks characteristic of individual europium(III) ion environments. The technique may be used to characterize the species present in complex equilibria in solution or to study europium(III) binding to macromolecules. Distinct europium(III) binding sites in thermolysin with long and short excited state lifetimes are observed.
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PMID:Time-resolved europium(III) excitation spectroscopy: a luminescence probe of metal ion binding sites. 50 7

Tick-borne encephalitis virus was treated with pronase or thermolysin. The resulting particles were banded in sucrose gradients and analyzed for polypeptide composition. Both enzymes caused a reduction in particle density from 1.19 to 1.15--1.16 g/cm3. No loss of viral lipid or nucleic acid could be observed. SDS-polyacrylamidegel electrophoresis showed that only the core protein V2 was unchanged whereas the envelope proteins V3 and V1 had disappeared from their original positions in the PAGE profile. Instead a new peptide(s) with molecular weight of 4000--6000 was found in which hydrophobic amino-acids were enriched. Crosslinking by dimethyl-3.3'-dithiobispropionimidate (DTBP) made the virus resistent to solubilization of the envelope proteins by TX-100. This could be interpreted by the formation of a dense envelope protein network around the nucleocapsid preventing its liberation by TX-100. Some data however indicate that direct crosslinking of at least one of the envelope proteins with the core cannot be excluded.
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PMID:Protease treatment and chemical crosslinking of a flavivirus: tick borne encephalitis virus. 50 94

The complete primary structure of the coat protein of strain VRU of alfalfa mosaic virus (AMV) is reported. The strain is morphologically different from all other AMV strains as it contains large amounts of unusually long virus particles. This is caused by structural differences in the coat protein chain. The amino acid sequence has mainly been established by the characterization of peptides obtained after cleavage with cyanogen bromide and digestion with trypsin, chymotrypsin, thermolysin or Staphylococcus aureus protease. The major sequencing technique used was the dansyl-Edman procedure. The VRU coat protein consists of 219 amino acid residues corresponding to a molecular weight of 24056. Compared to the coat protein of strain 425 [Van Beynum et al. (1977) Eur. J. Biochem. 72, 63-78], 15 amino acid substitutions were localized. Most of them have a conservative character and may be explained by single-point mutations. A correction is given for the AMV 425 coat protein: Asn-216 was shown to be Asp-216. The prediction of the secondary structure for the two viral coat proteins was not significantly influenced by the various amino acid substitutions except for the region containing residues 65-100. This led us to the hypothesis that the AMV coat protein may occur in two different conformations favouring its incorporation into either a pentagonal or hexagonal quasi-equivalent position in the lattice of the protein shell. The substitutions in the above-mentioned region of the VRU coat protein may have caused a strong preference for the hexagonal lattice conformation. The model is supported by preliminary sequence data of the same coat protein region in AMV 15/64, a strain morphologically intermediate between 425 and VRU.
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PMID:The primary structure of the coat protein of alfalfa mosaic virus strain VRU. A hypothesis on the occurrence of two conformations in the assembly of the protein shell. 52 Mar 17

The production, purification and analysis of peptide derived by digestion of mitochondrial aspartate aminotransferase with thermolysin and chymotrypsin are described. Despite the complexity of the peptide mixture obtained and the relative shortness of the fragments produced, these digests proved to be very useful for the completion of the primary structure determination of the enzyme. In fact, information for 87% of the total structure was contributed by thermolytic peptides, and for 89% by the chymotryptic ones. Moreover some of these peptides were essential for elucidating controversial points of the sequence.
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PMID:The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage with thermolysin and chymotrypsin. 55 5

1. Pig heart lipoamide dehydrogenase (NADH: lipoamide oxidoreductase, EC 1.6.4.3) has been immobilised to Sepharose by thiol-disulphide interchange via a series of thiolated spacer molecules of increasing length. A number of properties of the immobilised enzyme have been investigated in order to ascertain the effects of proximity to the matrix backbone. 2. Proximity to the matrix backbone reduced the specific activity for lipoamide as substrate but enhanced by 3-8-fold the diaphorase activity with 2,6-dichloroindophenol. These observations are explained in part by an increase in the apparent Km for lipoamide when the enzyme is covalently attached to Sepharose via a short spacer molecule. 3. Both the thermal stability at 90 degrees C and the stability in 30% (v/v) dioxane are enhanced by up to 200% when the enzyme resides close to the matrix but approach those of the native enzyme as the length of the spacer molecule is increased. 4. These data have been correlated with measures of the accessibility of the enzyme as the nominal length of the spacer arm was increased. Thus, as the chain length increased, the rate of cleavage of the disulphide linkage between the enzyme and spacer increased and the enzyme became more susceptible to proteolysis by thermolysin. In contrast, increasing the chain length of the spacer made the enzyme less amenable to inhibition by a specific antibody. 5. These data are discussed in terms of the effect of the matrix on the conformation of the bound enzyme.
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PMID:Immobilised lipoamide dehydrogenase. 2. Properties of the enzyme immobilised to agarose through spacer molecules of various lengths. 56 Sep 66

The amino terminus of bovine rhodopsin is blocked and has the sequence x-Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys-Thr-Gly-Val-Val-Arg, where CHO represents sites of carbohydrate attachment. The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala. Upon short-term digestion of rod outer segment (ROS) membranes with thermolysin, opsin (similar to 35,000 daltons) is converted to a membrane-bound fragment O' (similar to 30,500 daltons) and 2 peptides containing 12 amino acids are released from the carboxyl terminus of rhodopsin into the supernatant. Upon long-term digestion of ROS with thermolysin, opsin and O' are replaced by the membrane-bound fragments F1 (similar to 25,000 daltons), and F2 (similar 9,500 daltons). When 32P-ROS are digested, F2 carries the 32P. Both O' and F1 contain the amino-terminal glycopeptide.
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PMID:The amino- and carboxyl-terminal sequence of bovine rhodopsin. 59 23

1. Crude extracts of Limulus CNS cause hyperglycemia in Orconectes immunis and expand chromatophores in Uca pugilator. 2. The hyperglycemic action is due to a previously unknown polypeptide (LHGF) with an estimated molecular weight of 6400 daltons. LHGF is inactivated by hydrogen peroxide, pepsin, and protease, but unaffected by trypsin and brief boiling.3. The chromatophorotropic activity is due to the previously reported substance, LUC. LUC is shown to be a peptide with an approximate molecular weight of 1850 daltons; it is inactivated by hydrogen peroxide, protease, pepsin, trypsin, chymotrypsin, and thermolysin. 4. LUC and LHGF activity can be readily separated by gel filtration on a Sephadex G-25 column. 5. The similarity of LUC and LHGF to known crustacean hormones is dicussed.
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PMID:Separation and partial purification of central nervous system peptides from Limulus polyphemus with hyperglycemic and chromatophorotropic activity in crustaceans. 62 59

1. The isolation of the ADP/ATP translocator from beef heart mitochondria as the bongkrekateprotein complex is described, using hydroxyapatite chromatography and gel filtration in Triton X-100 solution. 2. The inhibitor is bound to the protein prior to solubilization with detergent for protection against denaturation. Only the intact bongkrekate-protein passes easily through the hydroxyapatite column. Bongkrekate shileds the protein in contrast to carboxyatractylate only partially against proteinases present in the crude extract. 3. The isolated bongkrekate protein shows the same molecular weights in dodecylsulfate and Triton X-100, the same amino acid composition and the same isoelectric point as the earlier isolated carboxyatractylate-protein complex. It differs by its higher sensitivity against trypsin and thermolysin. 4. The identity of both proteins is demonstrated by interconversion of the bongkrekate-protein into the carboxyatractylate-protein. The process requires the catalysis by ADP or ATP, the natural substrates of the protein. 5. The formation of the extractable [3H]bongkrekate-protein complex in mitochondria requires the presence of ADP or ATP. 6. These data, the immunological studies presented earlier, and the differences in the reactivity of -SH groups of the isolated bongkrekate and carboxyatractylate complexes (to be published) indicate that both proteins represent different conformational states of the translocator protein (m-state and c-state).
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PMID:Isolation of the ADP/ATP translocator from beef heart mitochondria as the bongkrekate-protein complex. 64 34

1. Normal carboxylic acids of different hydrophobicities and similar chain lengths were prepared and used for the modification of amino groups of thermolysin (EC 3.4.24.4). They were 4,7,10,13-tetraoxatetradecanoic acid, 4,7,10-trioxatetradecanoic acid, 4,7-dioxatetradecanoic acid and 4-oxatetradecanoic acid. 2. The modified enzymes were isolated by gel filtration. They had 6--7 acyl groups per molecule. Acylation of amino groups with 4-oxatetradecanoic acid and tetradecanoic acid made the enzyme insoluble. 3. The most hydrophilic enzyme derivative had similar enzyme activity and higher heat resistance than the native enzyme. The most hydrophobic derivative showed lower Km (50%) and V (40%) values for proteinase activity and lower heat resistance than the former derivative. The trioxa-derivative had intermediate characteristics. The results are discussed with respect to effects on stability and activity of the enzyme.
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PMID:Effect of hydrophobicity of acyl groups on the activity and stability of acylated thermolysin. 66 81

The complete amino acid sequence (128 residues) of the chicken erythrocyte histone H2A was deduced from the data provided by structural studies on the tryptic peptides from the maleylated histone and of the peptides obtained by thermolysin digestion of the native protein. The sequence of chicken histone H2A differs from the calf homologous histone by the deletion of one residue of histidine at position 123 or 124 and three conservative substitutions: a residue of serine replaces a residue of threonine at position 16, a residue of aspartic acid replaces a residue of glutamic acid at position 121 and a residue of alanine replaces a residue of glycine at position 128.
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PMID:Primary structure of chicken erythrocyte histone H2A. 66 68


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