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  • 1
    Electronic Resource
    Electronic Resource
    REGIONAL AND SUBCELLULAR DISTRIBUTION OF PROTEIN CARBOXYMETHYLASE IN BRAIN AND OTHER TISSUES (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 26 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Protein carboxymethylase, an enzyme that transfcrs the methyl group of S-adenosyl-L-methionine to carboxyl groups of proteins and endogenous acceptor proteins were examined in nerve and endocrine tissues. The highest protein carboxymethylase activity was found in the brain, followed by the testis, pituitary and heart. On the other hand, the tissue with the highest level of endogenous substrate(s) was the pituitary. The nearly identical specific activity ratio for two different protein substrates in all tissues examined, suggests that one enzyme is responsible for carboxymethylase activity in different tissues. The subcellular distribution of the enzyme in brain showed a high concentration in the soluble fraction, presumably representative of the enzyme in the cytosol of cell bodies. Considerable enzyme activity was also found in brain synaptosomes which was increased by osmotic lysis. Protein carboxymethylase was shown to accumulate proximally to a ligation of the rat sciatic nerve. A possible physiological role for protein carboxymethylase in neuronal function is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb07001.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The Regulation of Enkephalin Levels in Adrenomedullary Cells and Its Relation to Chromaffin Vesicle Biogenesis and Functional Plasticity (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 493 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb27216.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of a 7B2-derived tridecapeptide from bovine adrenal medulla chromaffin vesicles (1993)
    Springer
    Cellular and molecular neurobiology 13 (1993), S. 271-278 
    Details
    ISSN: 1573-6830
    Keywords: adrenal gland ; chromaffin vesicles ; 7B2 ; secretary peptide ; posttranslational processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. A novel tridecapeptide was isolated from extracts of bovine adrenal medulla chromaffin vesicles and the primary structure determined to be SVPHFSDEDKDPE. 2. This peptide is identical to the C termini of human and porcine 7B2 and is highly homologous to the same region of the mouse andXenopus lavis protein. 3. In all these species the homologous peptide is preceded by a pair of lysine residues, a potential proteolytic processing site. 4. Ser6 is part of a well-conserved casein kinase II consensus phosphorylation sequence. Evidence for phosphorylation of this residue was obtained during Edman sequencing. 5. Thus, this novel adrenal medullary probably arises from the posttranslational processing of the bovine 7B2 protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00733755
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  • 4
    Electronic Resource
    Electronic Resource
    Proteolysis at the secretase and amyloidogenic cleavage sites of theβ-amyloid precursor protein by acetylcholinesterase and butyrylcholinesterase using model peptide substrates (1993)
    Springer
    Cellular and molecular neurobiology 13 (1993), S. 279-287 
    Details
    ISSN: 1573-6830
    Keywords: Alzheimer's disease ; β-amyloid precursor protein ; acetylcholinesterase ; β/A4 peptide ; secretase ; amyloidosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. It was recently proposed that acetylcholinesterase (AChE), in addition to its esteratic activity, has proteolytic activity such that it may cleave theβ-amyloid precursor (β-APP) within theβ-amyloid sequence. The purpose of this paper was to examine further whether AChE or butyrylcholinesterase (BuChE) had associated proteinase activity that was involved in the metabolism ofβ-APP. 2. The ability of various preparations of AChE and BuChE to hydrolyze two synthetic fragments ofβ-APP695 as model substrates containing the normal and aberrant cleavage sites was studied. 3. Digestion of these synthetic substrates with commercial preparations ofElectrophorus electricus AChE indicated the presence of a trypsin-like proteolytic activity cleaving each peptide at the carboxy-terminal side of an internal lysine residue. 4. Purification of the trypsin-like proteinase activity by aminobenzamidine affinity chromatography yielded a preparation that was devoid of AChE activity but retained all of the proteinase activity. 5. Amino-terminal sequence analysis of this preparation showed that the first 13 amino acid residues were identical toβ-pancreatic trypsin. 6. These data indicate that the proteinase activity found in these commercial preparations of AChE is due to contamination with trypsin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00733756
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  • 5
    Electronic Resource
    Electronic Resource
    A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle (1990)
    Springer
    Cellular and molecular neurobiology 10 (1990), S. 507-523 
    Details
    ISSN: 1573-6830
    Keywords: adrenal gland ; chromaffin vesicles ; chromogranin B ; fast atom bombardment mass spectrometry ; secretogranin I ; secretory peptide ; posttranslational processing ; pyroglutamate ; pyrrolidone carboxylic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Following the recent demonstration of a glutaminyl cyclase activity localized in adrenomedullary chromaffin vesicles, an assay was developed to isolate and characterize posttranslationally modified peptides from this tissue which contain pyroglutamate. This assay consisted of spectrometric identification of peptides before and after enzymatic removal of pyroglutamyl residues. 2. Using this procedure, a pyroglutamyl peptide (BAM-1745) was isolated and sequenced and was shown to be a significant component of adrenomedullary secretory vesicles. 3. A computer search through the Swiss-Prot protein sequence database revealed a 93% identity of BAM-1745 and a fragment of human chromogranin B (Gln580-Tyr593).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712845
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    Paper (German National Licenses)
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