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R S Beck

Publications and source records attributed to R S Beck.

9 recordsLinked to original sources

Dizziness: state of the science.

Dizziness is prevalent in all adult populations, causing considerable morbidity and utilization of health services. In the community, the prevalence of dizziness ranges from 1.8% in young adults to more than 30% in the elderly. In the primary care setting, dizziness increases in frequency as a presenting complaint; as many as 7% of elderly patients present with this symptom. Classification of dizziness by subtype (vertigo, presyncope, disequilibrium, and other) assists in the differential diagnosis. Various disease entities may cause dizziness, and the reported frequency of specific diagnoses varies widely, depending on setting, patient age, and investigator bias. Life-threatening illnesses are rare in patients with dizziness, but many have serious functional impairment. Dizziness can be difficult to diagnose, particularly in elderly persons, in whom it often represents dysfunction in more than one body system. Given the relatively underdeveloped state of the empirical literature on dizziness, investigators would benefit from use of consistent criteria to describe dizziness symptoms and establish diagnoses. Investigation of the effects of testing and treatment should focus on diagnoses that are life threatening or lead to significant morbidity. In the elderly, a function-oriented approach should be studied and compared with current diagnosis-focused strategies. Alternative therapies for chronic and recurrent dizziness also merit investigation.

Algorithms↗

Access to care.

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Health Services Accessibility↗

JCAHO.

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Accreditation↗

Cellulase of Neurospora crassa.

Mycelia and ungerminated conidia of Neurospora crassa were found to secrete extracellular endocellulase (EC 3.2.1.4). A simple induction system of potassium phosphate buffer (ph 6.0) plus inducer relied on the internal metabolic reserves of conicia or mycelia to provide energy and substrates for protein synthesis. Buffer concentration for optimum enzyme production was 100 mM, but at higher buffer concentrations enzyme production was inhibited. Cellobiose was clearly the best inducer, with an optimum effect from 0.05 to 1 mM. In deionized water, cellulase remained mostly associated with the cell, but a variety of salts stimulated the release of cellulase into the medium.

Acetylglucosamine↗

Induction of beta-glucosidases in Neurospora crassa.

The induction of beta-glucosidases (EC 3.2.1.21) was studied in Neurospora crassa. Cellobiase was induced by cellobiose, but other inducers had little effect on this enzyme. Cellobiase activity was very low in all stages of the vegetative life cycle in the absence of di-beta-glucoside inducer. Aryl-beta-glucosidase was semiconstitutive at late stages of culture growth prior to conidiation. At early stages, aryl-beta-glucosidase was induced by cellobiose, laminaribiose, and gentiobiose, and weakly induced by galactose, amino sugars, and aryl-beta-glucosides. The induction properties of the beta-glucosidases are compared with those of the other disaccharidases of Neurospora. The induction of beta-glucosidases was inhibited by glucose, 2-deoxy-d-glucose, and sodium acetate. Sodium phosphate concentrations between 0.01 and 0.1 M stimulated induction of both enzymes, while concentrations above 0.1 M were inhibitory. The optimal condition for induction of both beta-glucosidases was pH 6.0. Cellobiase induction was relatively more inhibited than aryl-beta-glucosidase in the range of pH 6.0 to 8.0.

Cell-Free System↗

Localization of the beta-glucosidases in Neurospora crassa.

The beta-glucosidases (EC 3.2.1.21) of Neurospora crassa were studied with respect to their location in conidia and young mycelia. Aryl-beta-glucosidase of conidia was nearly equally divided between extracellular and bound activity. Bound aryl-beta-glucosidase was almost all available to substrate. An induction procedure was used to maximize both beta-glucosidases in 4 to 6-hr cells. Aryl-beta-glucosidase was entirely bound but still mostly (90%) detectable, whereas cellobiase was mostly internal and cryptic. A freeze-thaw cycle or treatment with phenethyl alcohol or deoxycholic acid made the cellobiase detectable without releasing it from the cell. A 10 to 20% increase in cell-bound aryl-beta-glucosidase could be obtained by this treatment. Dilute HCl (0.1 n) destroyed the patent aryl-beta-glucosidase but not the cryptic aryl-beta-glucosidase or the cryptic cellobiase activity in intact cells. This suggested that most aryl-beta-glucosidase activity was exterior to the cell membrane but still within the mural space. The thermal stability of patent aryl-beta-glucosidase and released cellobiase was found to be higher than in corresponding cell-free extracts. Measurements of K(m) suggested a slightly lower affinity for substrate p-nitrophenyl-beta-d-glucopyranoside by the enzymes in intact cells compared to enzymes in extracts.

Alcohols↗