Re-mediastinoscopy in the assessment of resectability of lung cancer.

OBJECTIVE: Thirty-one patients underwent re-mediastinoscopy in the diagnostic assessment of lung cancer. The reason for a repeat mediastinoscopy was either a negative result at the first operation in spite of CT indication of enlarged nodes or an incomplete first mediastinoscopy. METHODS: All patients underwent a conventional mediastinoscopy. RESULTS: In 22 patients with enlarged mediastinal lymph nodes at computed tomography, 10 had a positive lymph node histology at re-mediastinoscopy, while 12 were negative. In 9 patients with no enlarged mediastinal nodes at CT scan, but incomplete biopsies at the first mediastinoscopy, 1 patient had lymph node metastases. The median duration from the first to the second mediastinoscopy was 43 days. No major complications occurred. The staging of the patients was greatly affected by the re-mediastinoscopy. Of 31 patients judged as operable according to the initial mediastinoscopy only 60% were found to be operable following the second mediastinoscopy. CONCLUSION: This study has demonstrated the value of re-mediastinoscopy in assessment of resectability of lung cancer.

Toward a model for quality assessment in heart transplantation.

A model for quality assessment of heart transplantation that combines a scientific method for studying the recipients' quality of life and a basis for a method of clinical work by nurses and other health care professionals is discussed. Besides its use as a research method, this model also may serve as an instrument for documenting patients' biopsychosocial status, including coping capacity, and for evaluating nursing interventions.

The 1,4-beta-D-glucan glucanohydrolases from Phanerochaete chrysosporium. Re-assessment of their significance in cellulose degradation mechanisms.

A physico-chemical, functional and structural characterization, including partial sequence data, of three major 1,4-beta-D-glucan glucanohydrolases (EC. 3.2.1.4) isolated from the culture filtrate of the white-rot fungus Phanerochaete chrysosporium, shows that all three enzymes belong to a single family of cellulases. EG44, pI 4.3, (named after its apparent molecular mass in kDa), shows a clear homology with Schizopyllum commune Endoglucanase I (EGI); whereas EG38, pI 4.9, (named in the same manner) is related more closely to Trichoderma reesei (Trichoderma longibrachiatum) Endoglucanase III (EGIII). EG36, pI 5.6-5.7, is probably an EG38 protein lacking its cellulose binding domain. Strong synergistic action is induced by the enzymes acting in concert with cellobiohydrolases (CBHI and CBHII) from the same organism, indicating a highly effective enzymatic system for cellulose degradation. Controlled proteolysis with papain has allowed a so far unique cleavage of endoglucanases EG44 and EG38 into two domains: a core protein, which virtually lacks the capacity to absorb onto microcrystal-line cellulose but retains full catalytic activity against carboxymethyl cellulose and low molecular weight soluble substrates; and a peptide fragment corresponding to the cellulose binding domain. The latter appears to be of paramount significance in the mechanisms involved in the hydrolysis of microcrystalline cellulose.