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  • Blackwell Publishing Ltd  (565)
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  • 1987  (1,387)
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  • 1
  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The temporal cholesterolemic patterns to skim milk powder (SMP) and reprocessed SMP (RSMP) diets were compared to diets containing casein or laboratory rat chow over a 24-day period. SMP was hypocholestetemic relative to casein in rats fed a 1% dietary cholesterol. Reprocessing of SMP resulted in an apparent loss of the relative hypocholesterolemic reponse of native SMP. Amino acid analysis of SMP and RSMP, showed only marginally lower lysine levels than casein; however, the Iysine/arginine ratio was higher in SMP than either in casein or RSMP. Available lysine content in SMP was higher than in RSMP, suggesting occurrence of nonenyzmatic browning reactions. Although a similar cholesterolemic response was observed in casein and RSMP, the available lysine content of these two protein sources were markedly different, suggesting that reduced available lysine alone was not totally responsible for the lower cholesterolemic response of SMP, relative to casein.
    Type of Medium: Electronic Resource
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-03-06
    Description: Ribonuclease mitochondrial RNA processing, a site-specific endoribonuclease involved in primer RNA metabolism in mammalian mitochondria, requires an RNA component for its activity. On the basis of copurification and selective inactivation with complementary oligonucleotides, a 135-nucleotide RNA species, not encoded in the mitochondrial genome, is identified as the RNA moiety of the endoribonuclease. This finding implies transport of a nucleus-encoded RNA, essential for organelle DNA replication, to the mitochondrial matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, D D -- Clayton, D A -- GM-33088-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1178-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434997" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/*physiology ; Chemical Phenomena ; Chemistry ; Drug Resistance ; Endonucleases/isolation & purification/metabolism ; Enzyme Activation/drug effects ; *Genetic Code ; Humans ; Mammals/*genetics/metabolism ; Micrococcal Nuclease/pharmacology ; Mitochondria/*metabolism ; Oligonucleotides/pharmacology ; Organoids/physiology ; RNA/*biosynthesis/genetics/isolation & purification/physiology ; Ribonucleases/metabolism ; Subcellular Fractions/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1987-08-07
    Description: In situ measurements of the composition and spatial distribution of heavy thermal positive ions in the coma of comet Halley were made with the heavy-ion analyzer RPA2-PICCA aboard the Giotto spacecraft. Above 50 atomic mass units an ordered series of mass peaks centered at 61, 75, 91, and 105 atomic mass units were observed. Each peak appears to be composed of three or more closely spaced masses. The abundances decrease and the dissociation rates increase smoothly with increasing mass. These observations suggest the presence of chain molecules that are enriched in carbon, oxygen, and hydrogen, such as polyoxymethylene (polymerized formaldehyde), in comet Halley.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitchell, D L -- Lin, R P -- Anderson, K A -- Carlson, C W -- Curtis, D W -- Korth, A -- Reme, H -- Sauvaud, J A -- D'Uston, C -- Mendis, D A -- New York, N.Y. -- Science. 1987 Aug 7;237(4815):626-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17758562" target="_blank"〉PubMed〈/a〉
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1987-04-03
    Description: The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein with in vitro immunosuppressive properties, was determined through isolation and characterization of complementary DNA and genomic clones. The amino acid sequence encoded by one of the exons of the uromodulin gene has homology to the low-density-lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided that uromodulin is identical to the previously characterized Tamm-Horsfall glycoprotein, the most abundant protein in normal human urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennica, D -- Kohr, W J -- Kuang, W J -- Glaister, D -- Aggarwal, B B -- Chen, E Y -- Goeddel, D V -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):83-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3453112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Base Sequence ; Chemistry, Physical ; Cloning, Molecular ; Cysteine ; DNA/genetics ; Gene Expression Regulation ; Genes ; Glycoproteins/*genetics ; Humans ; Mucoproteins/*analysis/*genetics ; Peptide Fragments/analysis ; Physicochemical Phenomena ; RNA, Messenger/genetics ; Uromodulin
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  • 6
    Publication Date: 1987-09-11
    Description: A year-long monitoring program within an elongated channel-fan system in Bute Inlet of British Columbia, Canada, detected active sand-transporting turbidity currents. Measurements of bottom velocities and sediment collected in traps, as well as damage to moorings and equipment, captured the signatures of frequent energetic events. Maximum calculated velocities achieved were 335 centimeters per second, with flow thicknesses of more than 30 meters. Coarse sand was transported at least 6 to 7.5 meters above the sea floor. Turbidity currents flowed a minimum distance of 25.9 kilometers, but possibly as far as 40 to 50 kilometers, over bottom slopes of generally less than 1 degrees.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prior, D B -- Bornhold, B D -- Wiseman, W J Jr -- Lowe, D R -- New York, N.Y. -- Science. 1987 Sep 11;237(4820):1330-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17801471" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1987-02-20
    Description: The formation of clusters of altered axons and dendrites surrounding extracellular deposits of amyloid filaments (neuritic plaques) is a major feature of the human brain in both aging and Alzheimer's disease. A panel of antibodies against amyloid filaments and their constituent proteins from humans with Alzheimer's disease cross-reacted with neuritic plaque and cerebrovascular amyloid deposits in five other species of aged mammals, including monkey, orangutan, polar bear, and dog. Antibodies to a 28-amino acid peptide representing the partial protein sequence of the human amyloid filaments recognized the cortical and microvascular amyloid of all of the aged mammals examined. Plaque amyloid, plaque neurites, and neuronal cell bodies in the aged animals showed no reaction with antibodies to human paired helical filaments. Thus, with age, the amyloid proteins associated with progressive cortical degeneration in Alzheimer's disease are also deposited in the brains of other mammals. Aged primates can provide biochemically relevant models for principal features of Alzheimer's disease: cerebrovascular amyloidosis and neuritic plaque formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selkoe, D J -- Bell, D S -- Podlisny, M B -- Price, D L -- Cork, L C -- AG05134/AG/NIA NIH HHS/ -- AG06173/AG/NIA NIH HHS/ -- NS23340/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):873-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3544219" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Alzheimer Disease/pathology/*physiopathology ; Amyloid/immunology/*metabolism ; Amyloidosis/pathology/*physiopathology ; Animals ; Brain/pathology/*physiopathology ; Humans ; Immunoenzyme Techniques ; Macaca mulatta ; Pongo pygmaeus ; Saimiri ; Ursidae
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 1987-12-04
    Description: The relative positions of the centers of mass of the 21 proteins of the 30S ribosomal subunit from Escherichia coli have been determined by triangulation using neutron scattering data. The resulting map of the quaternary structure of the small ribosomal subunit is presented, and comparisons are made with structural data from other sources.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Capel, M S -- Engelman, D M -- Freeborn, B R -- Kjeldgaard, M -- Langer, J A -- Ramakrishnan, V -- Schindler, D G -- Schneider, D K -- Schoenborn, B P -- Sillers, I Y -- AI-09167/AI/NIAID NIH HHS/ -- AI-20466/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1403-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Brookhaven National Laboratory, Upton, NY 11973.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317832" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*analysis ; Escherichia coli/*ultrastructure ; Models, Structural ; Neutrons ; Ribosomal Proteins/*analysis ; Ribosomes/*ultrastructure
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  • 9
    Publication Date: 1987-01-23
    Description: The regional distributions of monoamine oxidase (MAO) types A and B have been identified in human brain in vivo with intravenously injected 11C-labeled suicide enzyme inactivators, clorgyline and L-deprenyl, and positron emission tomography. The rapid brain uptake and retention of radioactivity for both 11C tracers indicated irreversible trapping. The anatomical distribution of 11C paralleled the distribution of MAO A and MAO B in human brain in autopsy material. The corpus striatum, thalamus, and brainstem contained high MAO activity. The magnitudes of uptake of both [11C]clorgyline and L-[11C]deprenyl were markedly reduced in one subject treated with the antidepressant MAO inhibitor phenelzine. A comparison of the brain uptake and retention of the 11C-labeled inactive (D-) and active (L-) enantiomers of deprenyl showed rapid clearance of the inactive enantiomer and retention of the active enantiomer within MAO B-rich brain structures, in agreement with the known stereoselectivity of MAO B for L-deprenyl. Prior treatment with unlabeled L-deprenyl prevented retention of L-[11C]deprenyl. Thus, suicide enzyme inactivators labeled with positron emitters can be used to quantitate the distribution and kinetic characteristics of MAO in human brain structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fowler, J S -- MacGregor, R R -- Wolf, A P -- Arnett, C D -- Dewey, S L -- Schlyer, D -- Christman, D -- Logan, J -- Smith, M -- Sachs, H -- NS-15638/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 23;235(4787):481-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3099392" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Aged, 80 and over ; Brain/*enzymology ; Brain Stem/enzymology ; Cerebral Cortex/enzymology ; Clorgyline ; Corpus Striatum/enzymology ; Humans ; Monoamine Oxidase/*metabolism ; Selegiline ; Thalamus/enzymology ; Tomography, Emission-Computed
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  • 10
    Publication Date: 1987-07-03
    Description: The distribution of cells containing messenger RNA that encodes amyloid beta protein was determined in hippocampi and in various cortical regions from cynomolgus monkeys, normal humans, and patients with Alzheimer's disease by in situ hybridization. Both 35S-labeled RNA antisense and sense probes to amyloid beta protein messenger RNA were used to ensure specific hybridization. Messenger RNA for amyloid beta protein was expressed in a subset of neurons in the prefrontal cortex from monkeys, normal humans, and patients with Alzheimer's disease. This messenger RNA was also present in the neurons of all the hippocampal fields from monkeys, normal humans and, although to a lesser extent in cornu ammonis 1, patients with Alzheimer's disease. The distribution of amyloid beta protein messenger RNA was similar to that of the neurofibrillary tangles of Alzheimer's disease in some regions, but the messenger RNA was also expressed in other neurons that are not usually involved in the pathology of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bahmanyar, S -- Higgins, G A -- Goldgaber, D -- Lewis, D A -- Morrison, J H -- Wilson, M C -- Shankar, S K -- Gajdusek, D C -- AG05131/AG/NIA NIH HHS/ -- MH00519/MH/NIMH NIH HHS/ -- NS23038/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 3;237(4810):77-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299701" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics ; Amyloid/*genetics ; Amyloid beta-Peptides ; Animals ; Brain/*physiopathology ; Cerebral Cortex/physiology ; Gene Expression Regulation ; Hippocampus/physiology ; Humans ; Macaca fascicularis ; Nucleic Acid Hybridization ; RNA, Messenger/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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