Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.25.1 (proteasome)
28,817 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mutations affecting quantitatively the production of the sporulation-associated extracellular alkaline protease were isolated and characterized. They fall into at least five genes, three of which, ScoA, B and C, were mapped in the argC-metC region. The pleiotropic effects of these mutations concern several or all of the following: rate and timing of protease production, synthesis of alkaline phosphatase, time-course of spore formation. Electron microscopic evidence indicates delayed switch from one morphological stage to another. The nature of the Sco mutations and the genetic regulation of sporulation are discussed.
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PMID:Pleiotropic control mutations affecting the sporulation of Bacillus subtilis. 11 99

Seven female patients with amenorrhea, galactorrhea, and hyperprolactinemia were examined before and after selective transsphenoidal removal of a PRL-secreting microadenoma. Before adenomectomy, metoclopramide (MCP; 10 mg orally) and TRH (200 micrograms iv) did not increase PRL blood levels in any of the seven patients. On the contrary, after oral administration of 10 mg MCP, a positive response was noted in a group of eight lactating women 3 days postpartum. After surgery, serum PRL level returned to normal in all patients. A positive PRL response to MCP and TRH was found in six of the seven patients 1 month after surgery. One patient, who had the lowest PRL level, failed to show a PRL increase after both stimuli. These findings indicate that hypothalamic pituitary function can be restored to normal after transsphenoidal removal of PRL-secreting pituitary tumors.
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PMID:Serum prolactin response to thyrotropin-releasing hormone and metoclopramide in patients with prolactin-secreting tumors before and after transsphenoidal surgery. 12 21

The late type contact sensitizing effect of alkaline protease enzymes (PE) on the intact human skin has been investigated in the present study. The immune process of sensitisation was induced with "Tenzym prilled" (TP, Grindstedvoerket) and with "Maxatase" (M, Gist-Brocades) protease enzymes in the epicutaneous test (ET), using concentration series and various durations of application. The ETs were made on the intact (symptom-free) skin, as well as under conditions promoting the subcorneal penetration of PE. Challenge was carried out at 21 to 30 days following induction of 2092 subjects, and at 2 to 5 months on 1624 subjects. Despite the large number of subjects tested, contact sensitisation developed in none of the cases, although the inducing exposure took place under conditions promoting the immune process of sensitisation. In 60 individuals suffereing from occupational dermatitis on regular contact with PE and having no symptoms of early type inhalative allergy (mucous membrane changes, bronchial asthma-like symptoms) were challenged also by the intradermal test. No reaction was noted in any of them at 10 and 30 minutes, as well as at 24 and 48 hours following the test. Next the influence of PE is analysed in the induction or increased severity of the irritation caused by bioactive laundry detergents. The studies involved the use of serial dilutions of "Biopon" (Bn) laundry detergent containing TP or M, or not containing PE, respectively, by means of the ET. A total of 740 series (5220 tests) of the three variants were applied in dilution series to intact skin surface, as well as to pathologically and arteficially lsioned skin areas. The Bn variants containing and not containing PE increased the number of irratative reactions in essentially the same degree. This suggests that the irritative effect is not due to the presence of PE, but to the laundry-active detergents (WAS) of Bn in the first place, and to a lesser extent to its other ingredients.
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PMID:Skin irritancy and sensitivity to laundry detergents containing proteolytic enzymes. Part II. 12 49

Four natural protease inhibitors have been partially purified by heat treatment, ion-exchange chromatography pand gel filtration from Neurospora crassa. The inhibitory activity has been estimated by measuring the inhibition of proteolysis of casein as well as by the protection of Neurospora tryptophan synthase from proteolytic inactivation. The inhibitors are all oligopeptides and possess molecular weights in the range 5000-24 000 and appear to be very specific to Neurospora proteases. They may be classified into two types. The first are specific to Neurospora alkaline protease and the second to acidic protease. None of them exhibited any effect on other proteases including trypsin, chymotrypsin, papain, pepsin, thermolysin, subtilisin and proteinase K. The possible physiological role of these inhibitors is discussed.
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PMID:Isolation of specific protease inhibitors from Neurospora crassa. 13 53

Yeast lytic system produced by Arthrobacter GJM-1 bacterium during growth on baker's yeast cell walls contains a complete set of enzymes which can hydrolyze all structural components of cell walls of Saccharomyces cerevisiae. Chromatographic fractionation of the lytic system showed the presence of two types of endo-beta-1,3-glucanase. Rapid lysis of isolated cell walls of yeast was induced only by endo-beta-1,3-glucanase exhibiting high affinity to insoluble beta-1,3-glucans and releasing laminaripentaose as the main product of hydrolysis of beta-1,3-glucans. This enzyme was able to lyse intact cells of S. cerevisiae only in the presence of an additional factor present in the Arthrobacter GJM-1 lytic system, which was identified as an alkaline protease. This enzyme possesses the lowest molecular weight among other identified enzyme components present in the lytic system. Its role in the solubilization of yeast cell walls from the outer surface by endo-beta-1,3-glucanase could be substituted by preincubation of cells with Pronase or by allowing the glucanase to act on cells in the presence of thiol reagents. The mechanism of lysis of intact cells and isolated cell walls by the enzymes of Arthrobacter GJM-1 is discussed in the light of the present conception of yeast cell wall structure.
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PMID:Enzymes of the yeast lytic system produced by Arthrobacter GJM-1 bacterium and their role in the lysis of yeast cell walls. 33 91

Normal Escherichia coli bacteria are repelled by acetate, benzoate, and indole and attracted by alpha-aminoisobutyrate. We have isolated mutants that are attracted to acetate, benzoate, and indole and may be repelled by alpha-aminoisobutyrate. These reversed-taxis mutants are defective in a central processing component: a set of methylated proteins known as MCP 1. The mechanism of reversal of taxis is discussed.
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PMID:Attraction by repellents: an error in sensory information processing by bacterial mutants. 35 3

A comparison was made on the properties of the inclusion body proteins of two insect viruses: the nucleopolyhedrosis viruses of the European pine sawfly, Neodiprion sertifer, Geoffroy, and the gypsy moth, Lymantria dispar, Linnaeus. The inclusion body proteins were characterized by the following parameters: amino acid composition, polyacrylamide gel electrophoresis in the absence and presence of sodium dodecyl sulfate--mercaptoethanol, isoelectric focusing, and alkaline protease activity. The properties of the inclusion body proteins of the two viruses were similar in many respects, but clear differences were observed. A principal difference was the absence of alkaline protease activity associated with the inclusion body proteins of N. sertifer nucleopolyhedrosis virus.
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PMID:Comparative properties of the inclusion body proteins of the nucleopolyhedrosis viruses of Neodiprion sertifer and Lymantria dispar. 37 84

Circular dichroism (CD) spectra were measured for cytochromes P-450 (P-450) purified from phenobarbital- and 3-methylcholanthrene-induced rabbit liver microsomes. No striking difference in alpha-helix content was seen between phenobarbital-induced P-450 (PB P-450) (50%), phenobarbital-induced P-448 (PB P-448) (40%) and 3-methylcholanthrene-induced P-448 (MC P-448) (45--50%) in terms of ultraviolet CD spectra. Strong negative CD spectra associated with 3-methylcholanthrene transitions for MC P-448 in the near-ultraviolet region (250--310 nm) and weaker negative CD spectra associated with Soret transitions for PBP-448 ([theta] = 50 000) and MCP-448 ([theta] = 160 000), indicated that structures of these preparations are strikingly different from each other. Reduction of P-450 and P-448 led to a remarkable decrease of the Soret CD trough, suggesting that reduction was accompanied by a striking conformational change in the vicinity of the heme. Since CO complexes of reduced P-450 and P-448 showed a CD trough and an S-shaped CD, respectively, associated with the absorption peak at 450 nm, the heme vicinities are remarkably different from each other. The CD spectra in the visible region are also discussed. It was noticed that P-420, the denatured form of P-450, exhibited no CD spectra in the Soret and visible regions.
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PMID:Circular dichroism spectra of purified cytochromes P-450 from rabbit liver microsomes. 46 24

(1) RNase Ms was inactivated by iodoacetate. The inactivation was most rapid at pH 6.0, and was inhibited in the presence of a denaturant such as 8 m urea or 6 m guanidine-HCL. (2) Competitive inhibitors protected RNase Ms from inactivation by iodoacetate; the effect was in the order 2',(3')-GTP greater than 2',(3')-AMP, 2',(3')-UMP greater than or equal to 2',(3')-CMP. The order is not consistent with that of the binding constants of the 4 nucleotides towards RNase Ms (A is greater than C greater than G greater than U). (3) RNase Ms was inactivated with the concomitant incorporation of one molar equivalent of carboxymethly group. The following evidence indicated that the carboxymethyl group was incorporated into the carboxyl group of an aspartic acid or glutamic acid residue. (i) The carboxymethyl group incorporated into RNase Ms was liberated by treatment with 0.1 n NaOH or 1 m hydroxylamine. (ii) The amino acid composition of carboxymethylated RNase Ms (CM RNase Ms) after acid hydrolysis is similar to that of RNase Ms. (4) 14C-Labeled CM RNase Ms was digested successively with alkaline protease and amino-peptidase M. The radioactive amino acid released was eluted just before aspartate on an amino acid analyzer. After hydrolysis with 6 n HCL, glutamic acid was produced exclusively from the radioactive amino acid. The specific radioactivity of this amino acid calculated from the radioactivity and glutamic acid formed was practctically the same as that of CM RNase Ms. Thus, it was concluded that a carboxymethyl group was incorporated at the carboxyl group of a glutamic acid residue of RNnase Ms. (5) CM RNase Ms bound with 2'-AMP to the same extent as native RNase Ms, but bound to a lesser extent with 2',(3')-GMP. (6) Although the conformation of CM RNase Ms as judged from the CD spectrum was practically the same as that of native RNase Ms, the reactivity of CM RNase Ms towards dinitrofluorobenzene was different from that of native RNase Ms, indicating some difference in the conformation. (7) These results indicate that one glutamic acid residue is involved in the active of RNase Ms.
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PMID:Carboxymethylation of a minor ribonuclease from Aspergillus saitoi. 47 29

The steady-state kinetics of the alkaline mesentericopeptidase-catalysed hydrolysis of esters of the general formula Ac-X-OMe(OEt) has been studied, "X" being an amino acid residue (Ala, Val, Leu, Ile, Phe, Tyr, Trp, Lys). The values of the specificity ratio kcat/Km indicate that the bonds involving the carboxyl group of amino acids with aromatic and bulky aliphatic side chain are hydrolysed most effectively. On account of this, alkaline mesentericopeptidase is classified as a chymotrypisn-like alkaline protease. The primary specificity of mesentericopeptidase reveals the similarity of this enzyme to the group of subtilisins, as well as the distinctive characteristic feature of the enzyme to hydrolyse Ac-Leu-OMe with an efficiency practically equal to that of aromatic amino acid derivatives. Suggestions are made about the nature of the substrate-binding centre, taking into consideration Schechter's and Berger's concept of the secondary specificity.
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PMID:Primary specificity of alakaline mesentericopeptidase. Kinetic parameters for the hydrolysis of alpha-N-acetyl-L-amino acid methyl esters. 63 84


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