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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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: SUMMARY— A study was made of the fine structure of myofibril suspensions prepared from seven heifers immediately after death and after various times post-mortem. Studies on myofibrils sampled immediately after death showed that sucrose isolation gave the best structural preservation as indicated by maintenance of Z-line structure. Although the appearance of resting muscle was maintained in both sucrose and KCI preparations, several myofibrils from the KCI-treated preparations showed stretched sarcomeres. Glycerol-treated myofibrils usually had shorter sarcomere lengths than myofibrils prepared with the other two solvents. Although fibrillar preservation seemed adequate when glycerol was used, Z-line structure was seldom well-preserved with glycerol.Myofibrils from muscle sampled 24 hr post-mortem at 2°C were supercontracted with thick filaments pushed against or through the Z-line, and no trace of l-bands remained. Myofibrils from muscle sampled 24 hr post-mortem at 16°C were contracted, but to a much lesser extent than 2°C-24 hr myofibrils. Storage at 2°C for 312 hr after death resulted in myofibrils that were contracted and that were structurally in a much poorer state of preservation than their 16°C counterparts. The 16°C-312 hr myofibrils were slightly contracted as indicated by the absence of H-zones and the presence of prominent, although narrowed, I-bands. All observations showed that shortening accompanying rigor mortis caused changes in banding patterns similar, and probably identical, to those predicted by Huxley's sliding filament model for contracting muscle.
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  • 2
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– Investigations were conducted on the effect of three storage temperatures, 2°, 16°, and 37°, on the changes and relationships of certain chemical and physical properties of post-mortem bovine semitendinosus and psoas muscle. Post-mortem muscle shortening was measured with the isometer. Isometric tension development was maximal at 2°, minimal at 16°, and at 37° tension was approximately one-half that developed at 2°. The large tension development at 2° very likely originates from the same events as those in “cold shortening.” Differences in isometric tension parameters were noted between muscles in that psoas muscle developed tension and lost the ability to maintain tension more quickly than did the semitendinosus. Loss of ability to maintain tension was observed only at 2°, and this could correspond to a “resolution” of rigor mortis. Adenosine triphosphate (ATP) degradation was measured by two methods, ammonia production and bioluminescent enzymic method; the bioluminescent method proved to be the more satisfactory. A common relationship was observed between pH and ATP for both muscles and the three temperatures studied. No direct relationship was found between ATP degradation and shear resistance with the possible exception of muscle stored at 37°. Isometric tension parameters and shear resistance were related somewhat at 2° in semitendinosus muscle, but no relationship existed at 16° and 37°. Although considerable tension developed in psoas and semitendinosus muscle at 37°, shear resistance values decreased continuously, indicating that factors other than shortening are more important at high temperature and that these factors are temperature-dependent.The role of ATP degradation in tension development was difficult to interpret, since at 2°, only a small change occurred in ATP level during large tension development, and the level of ATP at 2° did not differ from ATP level in muscle stored at 16° which developed little tension.Differences in post-mortem muscle shortening at 2 and 37 are discussed.
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 34 (1969), 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: SUMMARY– Studies were conducted to investigate the effect of temperature on the actin-myosin interaction of rabbit and bovine muscle during rigor and post-rigor shortening. Muscle was stored at four different temperatures (2°, 16°, 25° and 37°), corresponding to three types of post-mortem muscle shortening: cold, minimal and high temperature. These three types of shortening are presumably related to different states of the actin-myosin interaction in post-mortem muscle. Post-mortem tenderization may be the result of either actin-myosin dissociation or F-actin depolymerization.To detect the occurrence of either of these possible changes, two salt solutions, differing widely in their myofibrillar protein extracting abilities, were used to compare post-mortem myofibrillar protein solubility after different times of post-mortem storage and to provide information about the actin-myosin complex. Myofibrillar protein solubility of both rabbit and beef muscle in 0.5M KCl, 0.1M phosphate, pH 7.4, increased markedly with increasing post-mortem storage at temperatures up to 25deg;. Similar solubility changes were obtained with 1.1M Kl, 0.1M K phosphate, pH 7.4, but these changes were much smaller in magnitude. Solubility in both salt solutions, in general, decreased for muscle stored at 37°.Although time and temperature of post-mortem storage caused appreciable alterations in protein solubility, these alterations could not be directly related to changes in tenderness or sarcomere length or to species differences in the effects of temperature on post-mortem shortening. Viscosity, analytical ultracentrifugation, and ATPase assays all indicated the absence of “normal” actomyosin in all myofibrillar protein extracts in this study. It was suggested that the 1.1 M KI extracts contained G-actomyosin, but the available evidence indicated the presence of only myosin in 3-hr, 0.5 M KCI extracts.
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  • 4
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– Proteolysis and its relationship to tenderness were studied by measuring nonprotein nitrogen (NPN), free amino groups, and shear resistance during post-mortem aging of bovine muscle. Both NPN and free amino groups increased during post-mortem aging, indicating some degradation of proteins and/or peptides. However, neither the increase in NPN nor free amino groups was related to post-mortem tenderization since these quantities increased only after most of the improvement in tenderness had occurred. Much of the increase in NPN or free amino groups may originate from degradation of sarcoplasmic proteins or peptides. It is suggested that weakening or breaks at crucial points in the sarcomere, such as at the junction of the Z-line with the thin filaments, occur within the first 48-72 hr post-mortem and that this weakening or cleavage is responsible for tenderization. Cathepsin D may be responsible for this weakening but most of the available evidence is against proteolysis as the primary cause of post-mortem tenderization.
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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: SUMMARY— Post-mortem changes in nucleoside triphosphatase activity of bovine myosin B have been studied by using several different modifiers with either 5 mM ATP or 5 mM ITP as substrate at ionic strengths (r/2) of 0.09, 0.19, or 0.52. Enzymic activity was determined by measuring the release of inorganic phosphate. There was very little difference in enzymic activity between myosin B isolated from prerigor, rigor (24 hr post-mortem) or post-rigor (312 hr post-mortem) muscle stored at either 2° or 16°C except that the specific activity of myosin B prepared from muscle stored for 12–24, hr post-mortem was higher than activity of myosin B prepared immediately after death. This increase cannot be explained in terms of rigor shortening, but suggests that a change in myosin conformation or in the nature of the actin-myosin interaction occurs in post-mortem muscle. If an actin-myosin interaction occurs during rigor mortis and if this association remains unchanged during extraction of myosin B, then the very low Mg++-modified myosin B enzymic activities obtained at Γ/2 = 0.19 and 0.52 indicate that this interaction is not irreversible. Extraction in the absence of ATP produced a myosin B whose ATPase activity was markedly inhibited by trace amounts of Mg++. This may be due to the absence of a-actinin in these myosin B preparations. No consistent differences in activation energies were found either at Γ/2 = 0.19 or 0.52 among the NTPase reactions of myosin B samples prepared from muscle after various times of post-mortem storage.
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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 structural appearance of homogenized myofibril suspensions from seven heifers was studied using phase microscopy at various times post-mortem with three different extracting solutions: 1) 0.25M sucrose, 1mM ethylenedi-aminetetraacetic acid (EDTA), 0.05M Tris-(hydroxymethyl) aminomethane (Tris), pH 7.6; 2) 0.15M KCI, 1mM EDTA, 0.05M Tris, pH 7.6; and 3) 50% glycerol, 1miZl EDTA, 0.05M Tris, pH 7.6. Samples were examined at death and 24 hr and 312 hr post-mortem with storage at 2 and 16°C. The 16°-24-hr samples exhibited a marked thickening of the A-band, a shortening of the l-band, and a replacement of the H-zone by a dark line or band. The 2°.24-hr samples showed only alternating light and dark bands of nearly equal width, which has been described as a typical supercontracted pattern. At 312 hr, more variability in banding pattern and fragmentation is encountered, but the trend is to preserve the pattern observed in the 24.hr samples. Occasionally, a narrow H-zone is seen in the center of a thickened A-band in the glycerol preparations sampled 312 hr post-mortem. The results suggest that cold shortening of bovine muscle is structurally identical to contraction and substantiate the view that shortening is minimal at 16° storage temperatures.The sucrose extracting solution consistently gave the best preservation and was used for subsequent experiments. Although banding patterns at death and in the 24-hr samples obtained with glycerol showed reliable consistency, these preparations at times exhibited a disturbing fuzziness. Results with KCI solutions were least desirable, because of repeatedly poor structural preservation, as indicated by variability in sarcomere lengths within and between fibers, as well as lack of clarity in banding.
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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: A study was made of the nucleosidetriphosphatase (NTPase) activities of myofibrils isolated from pre-rigor, rigor, and post-rigor bovine semitendinosus and psoas muscles with three different extracting solutions: 1) 0.25M sucrose, 1 mM ethylenediaminetetraacetic acid (EDTA), 0.05M trischydroxy-methyl)-aminomethane (Tris), pH 7.6; 2) 0.15M KCI, 1 mM EDTA, O.OSM Tris, pH 7.6; and 3) 50% glycerol, 1mM EDTA, 0.05M Tris, pH 7.6. Post-mortem storage was at 2 and 16°C. By 6 hr post-mortem, the Ca++- and Mg++-modified adenosine-triphosphatase (ATPase) activities at an ionic strength (I-/2) of 0.18 had increased 20–50% over the O-time level. An increase in Ca++-modified ATPase of Γ/2 = 0.52 was also found. The Mg++-modified inosinetriphosphatase (ITPase) at Γ/2 = 0.18 increased with post-mortem time, but the Cat+-modified ITPase at Γ/2 = 0.18 did not change.The Ca++-modified ITPase activity at Γ/2 = 0.52 increased for the first 24 hr post-mortem, but after 312 hr post-mortem, it had decreased back to the O-time level. No differences in NTPase activities were found between the semitendinosus and the psoas muscles or between post-mortem storage at 2 and 16°. Use of sucrose or KCI extracting solutions gave the most consistent NTPase results. The low Mg++-modified NTPase activity at Γ/2 = 0.52 suggests that it is possible to dissociate thick and thin filaments from rigor muscle through the use of 5mM ATP or ITP. The fact that NTPase activities in the presence of certain modifiers did not change with post-mortem time suggests that the increased NTPase activities did not result from a proteolytic loss of part of the enzyme molecule, causing an increased activity per unit of protein. Mg++-modified ATPase activities in the presence of a Ca++ chelator indicated that tropomyosin, the most sensitive of the three myofibrillar proteins to proteolytic degradation, had not undergone significant proteolysis, even after 312 hr post-mortem.
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  • 8
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 69 (1965), S. 293-297 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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: Post-mortem tension changes of rabbit psoas and beef geniohyoideus and semitendinosus muscle were studied. A special device was constructed and used to measure these changes while holding the muscle isometrically. It has been possible to demonstrate a pattern of tension development and cessation in rabbit muscle at 24°C and in beef muscle at 0°, 10°, and 24°C. With rabbit muscle no tension development was detected at 0° or 10°C. Initiation of tension development is affected by the ante-mortem state of the animal as well as by temperature. The post-mortem tension decline occurs after the disappearence of ATP and evidently is not related to ATP degradation. Possible relationships between post-mortem tension changes and meat tenderness are discussed.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Zoomorphology 59 (1967), S. 143-210 
    ISSN: 1432-234X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Summary 1. The brain of the ant Formica rufa has been studied (mushroom bodies; unstructured protocerebral neuropil, central body and deutocerebrum) with normal stains, silver impregnations, electron microscopy and lesions with subsequent degeneration of fibers. 2. The mushroom bodies mainly consist of four groups of nerve cells, differing in the location of the cell bodies and the structure of the dendritic arborizations. The axons of all these cells pass down the pedunculus; bifurcate and send branches to the \ga- and \gb-lobe. Little endings all over the axons are claimed to be synaptic regions. Lesions with following degeneration of the fibers show that axons of cell groups I and IV pass down to the \ga- and \gb-lobe in the middle of the neuropil. Groups II and III follow each other in the outer parts. \ldCentral endings\rd described by Trujillo-Cenoz and Melamed (1962) seem to belong to neurons from other lobes of the brain to the calyces, while the \ldthin fibers\rd are parts of mushroom body neurons. Terminations of neurons arising from other cells, connecting the mushroom bodies with sensory and motor lobes of the brain, are present all over the mushroom body neuropil. Endings in the calyx all show same structure. It could be pointed out that neurons of tracts originating from the antennal glomeruli and the lateral neuropil send arborizations in both calyces. Terminations of tracts ending in pedunculus, α- and β-lobe all are developped in the same manner, but differ from those in the calyx. Each ending is connected with many mushroom body neurons, covering a great part of the area of those lobes in cross sections. 3. Mushroom bodies, protocerebral bridge and central body are surrounded by a large mass of unstructured neuropil of the protocerebral lobes. In the anterior part of the protocerebrum the unstructured neuropil of both hemispheres is closely connected, but in the other parts a clear boundary between the two hemispheres exists and no connections \3- except few commissures \3- can be seen. Several different neuron systems have been found in the lateral lobes One system connecting the lobes with the calyces of the mushroom bodies and other tracts with arborizations in the pedunculus, one part entering the commissure dorsal of the central body, the other part terminating in the β-lobe of the other hemisphere. Further tracts are passing between ventral parts of the lateral neuropil and the central body. 4. The central body consists of three parts of neuropil, separated by cell-bodies. \ldHorizontal-systems\rd, fibers from the antennal glomeruli, lateral neuropil and \gb-lobes enter the sides of the central body neuropil, while \ldvertical systems\rd enter from ventral between the two \gb-lobes and dorsal, leaving the commissure between the two hemispheres. Two systems have been found connecting central body and mushroom bodies. Impregnations only show parts, so it is assumed that arborizations of these fibers also penetrate the unstructured protocerebral neuropil. 5. The antenno-motor center of the deutocerebrumis closely connected with protocerebral and subesophageal structures and shows equal distribution of neuropil unlike the sensory center, where synaptic glomerulus regions differ from the other parts of neuropil. The antennal nerve consists of about 60000 fibers, the major part entering the sensory center. Some fibers pass by and terminate in the antenno-motor neuropil. Three groups of fibers could be detected in the antennal nerve, but it only seems to be shure for one group (40000 fibers with 0,05-0,2 μ diameter per fiber) to function as sensory fibers. Each fiber only enters one glomerulus, so that each glomerulus is claimed to receive about 200 incoming antennal fibers. Outgoing tracts to other lobes of the brain are in connection with all parts of the sensory center and each fiber has its terminations in only one deutocerebral glomerulus. Segmental internuncials with cell-bodies lateral and medial of the neuropil unite several deutocerebral glomeruli. 6. Structure and function. It is tried to give some histological explanations for physiological results obtained by stimulation and lesions. Possible tracts for inhibition between the mushroom bodies and for connections between the mushroom bodies and the central body are enumerated. Structures and physiological results in the neuropil of the lateral protocerebral neuropil and their relations to the central body, pedunculi and calyces of the mushroom bodies are in accordance. The unstructured parts of the protocerebral neuropil seem to play an important coordinating role concerning integrative processes in the brain of insects.
    Notes: Zusammenfassung 1. Mit gew\:ohnlichen F\:arbemethoden, Metallimpr\:agnation, Elektronenmikroskopie und L\:asion mit Verfolgung der degenerierten Fasern wurde das Gehirn (Pilzk\:orper, Protocerebralloben, Zentralk\:orper und Deutocerebrum) der Ameise Formica rufa untersucht. 2. Im Pilzk\:orper wurden vier Zelltypen aufgefunden, die sich vor allem in der Lage der Zellk\:orper und der Struktur der Dendriten unterscheiden. Die Axone s\:amtlicher Zellen treten sowohl in den \ga- als auch \gb-Lobus ein. Kleine Stummel an den Axonen im Pedunculus, \ga- und \gb-Lobus werden als synaptische Bereiche angesehen. Durch L\:asionen konnte der Verlauf der Axone der einzelnen Zellgruppen verfolgt werden. Die von Trujillo-Cenoz u. Melamed (1962) beschriebenen “central endings” sind als Teile pilzkörperfremder Neuronen anzusehen, während die “thin fibers” den Dendriten der Pilzkörperneuronen angehören. Verzweigungen pilzkörperfremder Fasern finden sich in allen Teilen des Pilzkörperneuropilems. Die im Calyx endigenden Neuronen zeigen alle dieselbe Struktur. Für zwei Faserzüge wurde nachgewiesen, daß ihre Neuronen in beide Becher Verzweigungen abgeben und somit mit sämtlichen Becherbereichen in Verbindung stehen. Die Endigungen der pilzkörperfremden Systeme im Pedunculus, α- und β-Lobus weisen untereinander den gleichen Ban auf, unterscheiden sich aber von den Verzweigungen im Calyx. Jedes Neuron erfaßt einen größeren Teil der Querschnittsfläche. 3. Im frontalen Bereich des Protocerebrums sind beide Protocerebralloben eng miteinander verbunden, weiter zum \gb-Lobus bin trennen sie sich vollst\:andig. Auf der H\:ohe der \gb-Loben erfahren die Lateralloben ihre gr\:o\sBte Ausdehnung, da mehrere verschiedene Neurongruppen ausgebildet sind: Fasern von den Lateralloben zum Calyx, zum Pedunculus und von da zur Kommissur dorsal des Zentralk\:orpers und zum \ga-Lobus der Gegenseite, von den ventralen Protocerebrallobusbereichen zum Zantralk\:orper. Bemerkenswert ist die enge Verkn\:upfung mit den Pilzk\:orpern, vor allem aber ein System, das Protocerebralloben, Calyx, \ga- und \gb-Lobus miteinander verbindet. 4. Der Zentralkorper ist ein bilateralsymmetrisch aufgebautes Gebilde, in das \l"Horizontalsysteme\r" vom sensorischen Deutocerebralteil, vom Protocerebrallobus und von den \gb-Loben der Pilzk\:orper eintreten. „Vertikalsysteme” kommen von ventral und dorsal von der Kommissur zwischen den beiden Protocerebralhälften her. Zwei Systeme wurden aufgefunden, die die Zentralkörperteile mit den Pilzkörpern verbinden. 5. Der motorische Teil des Deutocerebrums steht in enger Verbindung mit dem Protocerebrum und dem Unterschlundganglion und weist keine auff\:alligen Neuropilemstrukturen auf. Im sensorischen Teil dagegen sind die Antennalglomeruli als die Synapsenbereiche gegen\:uber den \:ubrigen Fasermassen deutlich zu unterscheiden. Von der Antenne führen etwa 60000 Nervenfasern zum Deutocerebrum. Ein Teil davon zieht direkt durch zum motorischen Teil. Der Antennennerv besteht aus drei Fasergruppen. Sensorische Tätigkeit kann nur für eine Gruppe (40000 Fasern mit je 0,05-0,2 μ Durchmesser) mit Sicherheit angenommen werden. Jede Antennenfaser endet in nur einem Glomerulus. In jeden Glomerulus treten etwa 200 Antennenfasern ein. Jede der vom sensorischen Deutocerebralteil zu anderen Hirnbereichen weiterziehenden Nervenfasern steht nur mit einem Glomerulus in Verbindung, dock kommen die Fasern der einzelnen Bahnen aus sämtlichen Bereichen des sensorischen Deutocerebralteiles. Interneuronen im sensorischen Deutocerebralteil verbinden die einzelnen Glomeruli miteinander. 6. Struktur und Funktion. Es wird versucht, physiologische Befunde (elektrische Reizung, L\:asion) auf Strukturen im Insektengehirn zur\:uckzuf\:uhren. M\:ogliche Verbindungen f\:ur eine gegenseitige Hemmung der Pilzk\:orper werden genannt, Bahnen zwischen Pilzk\:orpern und Zentralkbrper sind ausgef\:uhrt. Strukturen und physiologische Befunde im Bereich der Protocerebralloben und ihre Beziehung zum Zentralk\:orper und zu den Pilzk\:orpern zeigen gro\sBe \:Ubereinstimmung. Den Protocerebralloben scheint eine wesentliche koordinative Beteiligung bei Verarbeitungsvorgängen im Insektengehirn zuzukommen.
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