Evaluation of energy spectral information in nuclear imaging and investigation of protein binding of cationic radionuclides by lactoferrin. Comprehensive progress report, October 1, 1977-September 30, 1980

Technical Report · Tue Jun 10 00:00:00 EDT 1980

DOI:https://doi.org/10.2172/6338006· OSTI ID:6338006

Hoffer, P. B.

Construction of an Anger camera-computer system which allows collection of both the position and energy signals from events detected by the scintillation camera has been completed. The system allows correction of energy response non-uniformity of the detector and facilitates research related to effects of energy discrimination in radionuclide scintigraphy. The system consists of electronic hardware to transmit and digitize the energy signal, software to record and process that signal in conjunction with spatial positioning signals, and additional hardware for recording the processed images so that they can be evaluated by observers. Preliminary results indicate that the system is useful in evaluating clinical images. Assymetric (eccentric) energy windows do improve image quality and are of value in improving detection of lesions on liver scintigraphs. The mechanisms by which Ga-67 is taken up in infection and tumor has been elucidated, and the uptake of radiogallium in microorganisms as a function of its interaction with siderophores was also studied. The primary function of these low molecular weight compounds is to trap ferric ion. However, gallium may be substituted for ferric ion and becomes trapped within the microorganism. The uptake of radiogallium by neutrophils and the role that lactoferrin plays in both intracellular localization of radiogallium and subsequent deposition of the radionuclide at sites of infection were also studied. Investigation of ferric ion analogs reveals definate differences in the affinity of these metals for binding molecules which helps explain their biologic activity. While ferric ion has the strongest affinity for such molecules, gallium has very high affinity for siderophores, moderate affinity for lactoferrin, and lower affinity for transferrin. The relative affinity of indium for these molecules is in approximately the reverse order.

• Research Organization: Yale Univ., New Haven, CT (USA). School of Medicine
• Sponsoring Organization: USDOE
• DOE Contract Number: AS02-78EV04625
• OSTI ID: 6338006
• Report Number(s): DOE/EV/04625-T1; ON: DE81025541; TRN: 81-013321
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
38 RADIATION CHEMISTRY, RADIOCHEMISTRY, AND NUCLEAR CHEMISTRY
LIVER
SCINTISCANNING
DATA PROCESSING
ABSCESSES
RADIONUCLIDE KINETICS
GALLIUM 67
BIOLOGICAL ACCUMULATION
LACTOFERRIN
LYMPHOCYTES
MICROORGANISMS
NEOPLASMS
TRANSFERRIN
TUMOR CELLS
CATIONS
METABOLISM
DIAGNOSTIC TECHNIQUES
BIOLOGICAL PATHWAYS
COMPUTERS
DIAGNOSIS
DIGESTIVE SYSTEM DISEASES
ENERGY DEPENDENCE
EQUIPMENT INTERFACES
GAMMA CAMERAS
RECORDING SYSTEMS
HODGKINS DISEASE
LYMPHOMAS
IRON COMPOUNDS
ANIMAL CELLS
BETA DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY
BODY FLUIDS
CAMERAS
CARBOHYDRATES
CHARGED PARTICLES
CONNECTIVE TISSUE CELLS
COUNTING TECHNIQUES
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
DISEASES
ELECTRON CAPTURE RADIOISOTOPES
GALLIUM ISOTOPES
GLANDS
GLOBULINS
GLOBULINS-BETA
GLUCOPROTEINS
INTERMEDIATE MASS NUCLEI
IONS
ISOTOPES
LEUKOCYTES
MATERIALS
METALLOPROTEINS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
PATHOLOGICAL CHANGES
PROCESSING
PROTEINS
RADIOISOTOPE SCANNING
RADIOISOTOPES
SACCHARIDES
SOMATIC CELLS
TRANSITION ELEMENT COMPOUNDS
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560174 - Radiation Effects- Nuclide Kinetics & Toxicology- Microorganisms- (-1987)
400702 - Radiochemistry & Nuclear Chemistry- Properties of Radioactive Materials