ABSTRACT
The Laboratory Information System (LIS) was designed as a "turn-key" system. The main functions are operated interactively on a mini-computer which gives the laboratory complete control over daily processing. Collection of results from automated analyzers is accomplished via a micro-computer/micro-processor network. Links are provided with a central main frame computer for immediate patient identification and historical data processing. LIS is designed to manage all the operations involved in laboratory activities. The system has 14 major functions: registration of test requests, production of specimen collection sheets and identification labels, confirmation of specimen collection, production of aliquot labels, workload inquiry, production of worksheets, manual entry of test results, automated entry of test results, results inquiry, preliminary report, final report, daily activities reports, statistical reports, billing. System security is provided along three directions: data entry validation, system access control, and memory protection. The main advantages of LIS are: reduced clerical work, better evaluation of workload, faster communication, improvement of information given to the clinician: adapted reference values, interpretation, comments, improved retrieval operations, faster billing.
Subject(s)
Information Systems/instrumentation , Laboratories , Autoanalysis , Computers , Costs and Cost Analysis , Laboratories/economicsABSTRACT
In vitro binding of growth hormone was characterized in rat liver. Microsomal preparations were found more active than membranes purified with an aqueous two-phase polymer system. Binding conducted at 4 degrees C was found optimal after 72 hours of incubation in 5 mM Tris-Maleate buffer pH 6.4 with 25 mM CaCl2. Injecting estrone (25 microgram/100 g B.W.) for one week induced the formation of lactogenic receptors, and increased the specific binding of hGH from 2.8 +/- 1.9 to 22.3 +/- 7.1%. Prolactin and hGH, but not rGH or other pituitary hormones, could displace radioactive hGH. With incubations conducted at 37 degrees C, equilibrium was reached more rapidly but at the cost of a more extensive degradation. The presence of membrane receptors in the medium partly protected the hormone against aggregation and degradation. Scatchard plots were obtained from experiments conducted under optimal conditions and analyzed on computer using a program based on an iterative method. Data indicated that lactogenic receptors possessed a single specific binding site for hGH with a constant (Ka) of 2.18 +/- 0.22 x 10(9) M-1 and a binding capacity of 304 +/- 91 fm/mg proteins.
