Participatory management at Boston's Beth Israel Hospital.

In the mid-1980s, the senior management of Boston's Beth Israel Hospital became concerned that continuous cost-cutting efforts could lower the quality of the hospital's services and the morale of its staff. This led them to investigate organizational approaches to "participatory management" to determine whether any of these might be of value to the hospital. They decided that an approach developed in the 1930s called the "Scanlon Plan" would be compatible with the workplace culture of Beth Israel, could help the hospital meet the ongoing problems of change, and could help the staff at all levels develop a sense that they owned the problems of quality, productivity, and efficiency, which would motivate them to address these problems constructively in the face of necessary budget constraints. This plan has two mechanisms to foster employees' positive participation: (1) a process to ensure that all members of the organization have the opportunity to improve productivity, primarily through an open suggestion system and a responsive committee structure, and (2) a means of providing equitable rewards for all members of the organization as productivity and quality improve. This essay describes in some detail the plan and why it was selected, explains how it was adapted, prepared for, and finally implemented in 1989, and reports its success, lessons learned, and future plans as of early 1992. The authors believe Beth Israel's experience with the Scanlon Plan is noteworthy as an example of a leading teaching hospital's taking a quality improvement program seriously and making it work.     

Focus on: Newark Beth Israel Medical Center Biomedical Engineering Department.

This paper describes the Biomedical Engineering Department of Newark Beth Israel Hospital. This hospital's extensive involvement in research, heart transplantation, and special technologies has placed unusual demands on the Biomedical Engineering Department because of the large volume of routine and specialized equipment involved. The 12-person Department is responsible for servicing over 2700 pieces of equipment in 91 various hospital departments, and also offers its services to other local hospitals. Established in 1970, the Department uses a computerized biomedical equipment database program to manage data for repairs, preventive maintenance, and electrical safety.     

A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype.

This study describes a patient with a thalassemia intermedia-like phenotype in whom beta-globin gene sequencing detected a novel abnormal hemoglobin (Hb) due to a T-C substitution at codon 114 of the beta-globin gene arising as a de novo mutation. The abnormal variant was designated Hb Brescia after the place of birth of the propositus. Normal sequences were detected at the in trans beta-globin locus. In addition, alpha-globin gene analysis detected a triple alpha-globin locus which was inherited from the father. The T-C change at position 114 of the beta-globin gene results in a leucine to proline substitution (Leu-Pro) in the G-helix. The resulting Hb tetramer is highly unstable and precipitates forming inclusion bodies in the peripheral red blood cells. Moreover, the Leu-Pro substitution interferes negatively with the four alpha 1 beta 1 contact points of the G-helix most likely adversely affecting the alpha beta dimer formation. The very severe phenotype presented by our patient is unusual in a heterozygote for an unstable Hb variant and may be explained by the coinheritance of the triple alpha-globin locus.     

Hemoglobin Cowtown (beta 146 HC3 His-Leu): a mutant with high oxygen affinity and erythrocytosis.

A new mutant, hemoglobin Cowtown, has been found in a white man and his father, both of whom have erythrocytosis. The father had previously been treated with 32P for polycythemia vera. The abnormal hemoglobin is not detectable on electrophoresis in alkaline buffers, but it resolves distinctively on electrophoresis in citrate agar, pH 6.0; similarly, the abnormal beta-globin chain does not separate from beta-A in urea 2-mercaptoethanol buffers of pH 8.9, but it moves anodically to beta-A at pH 6.0. Peptide chromatography and amino acid analysis of the beta chain reveal that the C-terminal histidine residue (beta 146) has been replaced by leucine. Like several other hemoglobins substituted at this residue, Hb Cowtown has a high oxygen affinity and a diminished Bohr effect.     

Hemoglobin A2 levels in health and various hematologic disorders.

Using a method involving elution of hemoglobin bands from cellulose acetate strips following electrophoresis of hemolysates, hemoglobin A2 (Ab A2) was quantitated in bloods from 300 healthy individuals and 904 patients. The percentage of Hb A2 was elevated in beta-thalassemia heterozygotes and some patients who had megaloblastic anemia. In the latter, the highest Hb A2 levels were observed in patients with the most severe anemia. Low Hb A2 percentages were found in iron-deficiency anemia, hereditary persistance of fetal hemoglobin, and Hb H disease. In iron-deficiency anemia, the lowest levels of Hb A2 were observed in association with the most severe anemia. Iron and folate deficiency each suppressed Hb A2 levels in beta-thalassemia heterozygotes; however, vitamin B12 deficiency did not alter the percentage of Hb A2 in thalassemia. Malignant tumors, renal and hepatic insufficiency, chronic infections and inflammation, hemolytic disease, lead poisoning, aplastic anemia, leukemia, myelofibrosis, and hypothyroidism did not change Hb A2 levels. The pathogenesis of altered Hb A2 levels and their clinical significance in various diseases are discussed.     

Exclusion of close linkage between the parathyroid hormone gene and a mutant gene locus causing idiopathic hypoparathyroidism.

A family is presented in which the mother has transmitted primary hypoparathyroidism with early onset and serum PTH (44-68) and C terminal deficiency to her two sons. Restriction enzyme analysis of allelic variation at the PTH gene locus revealed that the disease and the PTH alleles segregate independently. It is therefore concluded that the primary molecular defect leading to this form of hypoparathyroidism is not located within the PTH gene itself.     

A double heterozygous hemoglobin. Hemoglobin OIndonesia and hemoglobin DPunjab in an individual.

During surveys for abnormal hemoglobins in Iran, an individual was found to have four electrophoretically distinct hemoglobins. The abnormality was found only in the father of the propositus, in two of the father's sisters, and in three brothers and sisters of the propositus. Investigations revealed that the four hemoglobin components are the result of a double heterozygosity between an alpha-chain variant (Hb OIndonesia) and a beta-chain variant (Hb DPunjab). The presence of the abnormal hemoglobins was not associated with hemolytic disorders or obvious clinical symptoms.