Aim. The purpose of this systematic review was to determine the extent to which the research literature indicates body temperature norms in the geriatric population. Objectives. The specific questions addressed were to examine normal body temperature values in persons 60 years of age and older; determine differences in temperature values depending on non‐invasive measurement site and measurement device used; and, examine the degree and extent of temperature variability according to time of day and time of year. Background. The traditional ‘normal’ temperature of 98·6 °F/37 °C may in fact be lower in older people due to the ageing process. Age‐associated changes in vasomotor sweating function, skeletal muscle response, temperature perception and physical behaviours may influence the ability to maintain optimum temperature. Design. A systematic literature review. Methods. A search of multiple databases yielded 22 papers which met inclusion criteria. Studies were included which focused on temperature measurement, sampled persons 60 years of age and older, collected data from non‐invasive temperature measurement sites and which used a prospective study design. Studies were independently appraised using a structured appraisal format. Results. Temperature normal values by site were rectal 98·8 °F/37·1 °C, ear‐based 98·3 °F/36·8 °C, urine 97·6 °F/36·5 °C, oral 97·4 °F/36·3 °C and axillary 97·1 °F/36·2 °C. Temperature exhibited a 0·7 °F/0·4 °C diurnal and 0·2 °F/0·1 °C circannual variation. Conclusions. Synthesis of data indicated that normal body temperature values in older people by sites were rectal 0·7 °F/0·4 °C, ear‐based 0·3 °F/0·2 °C, oral 1·2 °F/0·7 °C, axillary 0·6 °F/0·3 °C lower than adults’ acceptable value from those traditionally found in nursing textbooks. Relevance to clinical practice. Given the fact that normal body temperature values were consistently lower than values reported in the literature, clinicians may need to re‐evaluate the point at which interventions for abnormal temperatures are initiated.

LPL is an enzyme involved in the breakdown and uptake of lipoprotein triglycerides. In the present study, we examined how the transgenic (Tg) overexpression of human LPL in mouse skeletal muscle affected tolerance to cold temperatures, cold-induced thermogenesis, and fuel utilization during this response. Tg mice and their nontransgenic controls were placed in an environmental chamber and housed in metabolic chambers that monitored oxygen consumption and carbon dioxide production with calorimetry. When exposed to 4°C, an attenuation in the decline in body temperature in Tg mice was accompanied by an increased metabolic rate (15%; P < 0.001) and a reduction in respiratory quotient (P < 0.05). Activity levels, the expression of uncoupling proteins in brown fat and muscle, and lean mass failed to explain the enhanced cold tolerance and thermogenesis in Tg mice. The more oxidative type IIa fibers were favored over the more glycolytic type IIb fibers (P < 0.001) in the gastrocnemius and quadriceps muscles of Tg mice. These data suggest that Tg overexpression of LPL in skeletal muscle increases cold tolerance by enhancing the capacity for fat oxidation, producing an avian-like phenotype in which skeletal muscle contributes significantly to the thermogenic response to cold temperatures.

maintained by living organisms. This is the condition of optimal functioning for the organism and includes many variables, such as body temperature and fluid In biology, homeostasis (British also homoeostasis; HOH-mee-ə-STAY-sis) is the state of steady internal physical and chemical conditions maintained by living organisms. This is the condition of optimal functioning for the organism and includes many variables, such as body temperature and fluid balance, being kept within certain pre-set limits (homeostatic range). Other variables include the pH of If an entity is homeostatically controlled it does not imply that its value is necessarily absolutely steady in health. Core body temperature is, for instance, regulated by a homeostatic mechanism with temperature sensors in, amongst others, the hypothalamus of the brain. However, the set point of the regulator is regularly reset. For instance, core body temperature in humans varies during the course of the day (i.e. has a circadian rhythm), with the lowest temperatures occurring at night, and the highest in the afternoons. Other normal temperature variations include those related to the menstrual cycle. The temperature regulator's set point is reset during infections to produce a fever. Organisms are capable of adjusting somewhat to varied conditions such as temperature changes or oxygen levels at altitude, by a process of acclimatisation. Homeostasis does not govern every activity in the body. For instance, the signal (be it via neurons or hormones) from the sensor to the effector is, of necessity, highly variable in order to convey information about the direction and magnitude of the error detected by the sensor. Similarly, the effector's response needs to be highly adjustable to reverse the error – in fact it should be very nearly in proportion (but in the opposite direction) to the error that is threatening the internal environment. For instance, arterial blood pressure in mammals is homeostatically controlled and measured by stretch receptors in the walls of the aortic arch and carotid sinuses at the beginnings of the internal carotid arteries. The sensors send messages via sensory nerves to the medulla oblongata of the brain indicating whether the blood pressure has fallen or risen, and by how much. The medulla oblongata then distributes messages along motor or efferent nerves belonging to the autonomic nervous system to a wide variety of effector organs, whose activity is consequently changed to reverse the error in the blood pressure. One of the effector organs is the heart whose rate is stimulated to rise (tachycardia) when the arterial blood pressure falls, or to slow down (bradycardia) when the pressure rises above the set point. Thus the heart…

[Fine structure and seasonal changes in the constant electrical field in man]. Fine structure of distribution of electric potential difference (EPD) in human skin of some points on arms, body and face relative to a referent point on the neck was investigated. Diurnal variations of EPD fine structure for individuals and seasonal differences expressed in an increase of the amplitude of variations and shift of EPD mean values to the positive region in winter as compared with summer were observed. The indicated peculiarities are connected with external factors and reflect changes of metabolic activity of organism living activity processes. Published in Biofizika

Long-term stability of multienzyme protein systems is governed by preservation of conformational integrity and resistance to thermally induced structural destabilization. This study evaluated bovine pancreatin (BP) obtained by conventional extraction (CM) and ultrasound-assisted extraction (UAM) during 0-930 days of storage at 10-40 °C. Amylolytic (AA), proteolytic (PA), and lipolytic activities (LA), representing the functional enzymatic activity (EA) of the multienzyme protein system, were monitored to characterize degradation kinetics and activity loss associated with conformational destabilization. After 930 days at 20 ± 1 °C, UAM retained 76% of initial AA compared with 58% for CM, corresponding to a 31% higher residual activity in UAM. LA demonstrated comparatively high stability in both preparations (~84% retention), whereas PA exhibited delayed degradation and significantly higher residual values in UAM samples. Two-way ANOVA confirmed significant effects of extraction method, storage duration, and their interaction (<i>p</i> < 0.001), indicating method-dependent kinetic behavior. Elevated temperatures (35-40 °C) accelerated inactivation, consistent with increased molecular mobility and reduced conformational stability. The smoother degradation trajectories and lower apparent inactivation rates observed in UAM preparations suggest kinetic stabilization, potentially associated with improved conformational preservation and reduced extraction-induced structural stress. Both preparations complied with pharmacopoeial microbiological limits. These findings support the hypothesis that UAM enhances long-term functional stability of complex multienzyme systems through mechanisms related to conformational resilience. As a system composed primarily of α-amylase, serine proteases (trypsin, chymotrypsin, elastase), and lipases, its functional performance depends on preservation of structural integrity and catalytic activity during storage [ 1 , 2 ]. Owing to its proteinaceous nature, pancreatin is inherently sensitive to environmental factors such as temperature, moisture, water activity, and oxygen exposure, which may induce In hydrated systems, water-mediated conformational mobility and disruption of intramolecular hydrogen-bond networks may further facilitate structural rearrangements and aggregation pathways [ 4 , 5 ]. In addition to physicochemical stability, microbiological quality is critical for maintaining product safety and functional performance [ 6 , 7 ]. Elevated moisture and water activity promote microbial proliferation and may accelerate structural degradation of enzymes, thereby compromising both stability and regulatory compliance. Because pancreatin represents a heterogeneous multienzyme system, its overall stability reflects the combined behavior of structurally distinct catalytic proteins rather than a single enzymatic component [ 13 , 14 , 15 ]. Although previous investigations have addressed short-term stability, thermal resistance, and pH-dependent activity of individual pancreatic enzymes, systematic long-term studies integrating storage duration, temperature effects, extraction technology, and microbiological quality assessment remain limited. In particular, quantitative data describing degradation kinetics in complex multienzyme systems over extended storage periods are scarce [ 2 , 3 ]. PA exhibited pronounced interaction effects, consistent with the known susceptibility of serine proteases to gradual inactivation and possible self-digestion during storage [ 11 , 12 , 13 ]. AA showed temperature sensitivity compatible with the structural role of Ca 2+ in maintaining conformational rigidity. In contrast, LA demonstrated comparatively high long-term stability, retaining approximately 84% of initial activity after 930 days in both preparations. Although the extraction method significantly influenced LA ( p < 0.001), the magnitude of difference was moderate, indicating enzyme-specific stability hierarchies within the multienzyme system [ 25 ]. The system functioned at a frequency of 20 kHz and was equipped with an MS 72 probe (13 mm tip diameter), which was immersed 1.5 cm into the sample. Ultrasonic processing was applied for 15 min in total. To avoid thermal inactivation of enzymes, the temperature of the extraction medium was maintained below 25 °C using an external ice bath. The pulsed sonication regime was selected to reduce heat accumulation and preserve enzyme activity while maintaining effective cavitation. The pause intervals between pulses allowed dissipation of thermal energy and promoted bubble regeneration, thereby improving cavitation efficiency and cell disruption. The hydrolysis process was carried out for 10 min using 6.0 units of enzyme activity at regulated pH and temperature parameters. One unit of AA was defined as the quantity of enzyme capable of converting 1 g of soluble starch into dextrins, corresponding to approximately 30–50% hydrolysis of the initial substrate. The resulting enzyme activity was expressed as units per gram of dry enzyme preparation ( AA / g ). The degree of starch degradation was determined using a colorimetric assay based on iodine–starch complex formation. The reduction in iodine staining intensity reflected the decrease in the amount of residual, non-hydrolyzed starch. While the present study provides comprehensive insights into the long-term stability of BP under defined storage conditions, certain limitations should be acknowledged. Continuous monitoring of water activity and potential structural changes in enzymes were not performed, and the findings are based primarily on activity-based assays. Additionally, storage conditions were controlled in the laboratory and may not capture all variations encountered in industrial or real-world settings. Future work incorporating broader physicochemical analyses and more diverse storage scenarios could further elucidate the mechanisms affecting enzyme stability. 6.

(b) Why has the entropy in the hot-cold system in the blue panel increased in the second image? 2. (a) Explain … determine enzyme activity? 4. In the pH experiment, the students measured the rate of enzyme activity by comparing … The temperature regulation center of the human body is in the hypothalamus of the brain which has a Favorite Share Flag Flag this item for Graphic Violence Explicit Sexual Content Hate Speech Misinformation/Disinformation Marketing/Phishing/Advertising Misleading/Inaccurate/Missing Metadata texts BIOZONE AP Biology 2 Student Workbook by Tracey Greenwood ; Lissa Bainbridge-Smith ; Kent Pryor ; Richard Allan Publication date Oct 16, 2017 Publisher BIOZONE International Ltd Collection internetarchivebooks ; printdisabled Contributor Internet Archive Language English Item Size 1.4G Notes /type/text Access-restricted-item true Addeddate 2024-02-23 14:45:58 Autocrop_version 0.0.15_books-20220331-0.2 Boxid IA40985602 Camera USB PTP Class Camera Collection_set printdisabled External-identifier urn:lcp:biozoneapbiology0000trac:epub:ef92d9bb-72e6-4c68-80b6-08d219db02ef urn:lcp:biozoneapbiology0000trac:lcpdf:51c85812-9b1c-4a83-b3a7-c4fce42c3da2 Foldoutcount 0 Identifier biozoneapbiology0000trac Identifier-ark ark:/13960/s268jm5csz4 Invoice 1652 Isbn 9781927309650 Metasource_catalog openlibrary Ocr tesseract 5.3.0-3-g9920 Ocr_detected_lang en Ocr_detected_lang_conf 1.0000 Ocr_detected_script Latin Ocr_detected_script_conf 1.0000 Ocr_module_version 0.0.21 Ocr_parameters -l eng Old_pallet IA409813 Openlibrary_edition OL36681455M Openlibrary_work OL27053868W Page-progression lr Page_number_confidence 53 Page_number_module_version 1.0.5 Pages 430 Pdf_module_version 0.0.22 Ppi 360 Rcs_key 24143 Republisher_date 20230614143640 Republisher_operator associate-russelpamela-maglasang@archive.org Republisher_time 730 Scandate 20230610095736 Scanner station40.cebu.archive.org Scanningcenter cebu Scribe3_search_catalog isbn Scribe3_search_id 9781927309650 Source removed Tts_version 5.7-initial-24-gde4a12cb Show More Show Less plus-circle Add Review comment Reviews 183 Views 1 Favorite Purchase options Better World Books DOWNLOAD OPTIONS No suitable files to display here.