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H Nelson

Publications and source records attributed to H Nelson.

At least 181 records · Page 10Linked to original sources

Abdominal wall hernias as a complication of peritoneal dialysis.

Home peritoneal dialysis has recently become an important addition to the therapy of chronic renal failure. Abdominal wall hernias have become more apparent as complications of this mode of dialysis, with isolated instances of incarcerations and one fatality. Results of our review of 276 patients receiving peritoneal dialysis revealed seven with hernias, an incidence of 2.5 per cent. Six patients with hernias were receiving c.a.p.d.; one patient was receiving c.c.p.d., and none was receiving i.p.d., for incidences of 17, 5 and zero per cent, respectively. All hernias found at presentation occurred within two to 20 months after peritoneal catheter placement. Most were ventral or umbilical, and all were repaired electively without serious complications. All patients with hernias had associated problems with leaks, peritonitis or predialysis hernias. In two of four patients with predialysis hernias, herniorrhaphy without catheter removal resulted in two recurrences. Abdominal wall hernias are a more frequent complication of c.a.p.d. and c.c.p.d., modalities which require large volumes of peritoneal dialysate during ambulatory hours. Review of the literature reveals that wound tensile strength and healing are decreased in those patients having renal disease with uremia, anemia and malnutrition. However, these factors do not increase the over-all incidence of hernias. Patients should be screened for hernias, and hernias should be repaired prior to catheter placement. Hernias presenting during dialysis are best treated by herniorrhaphy and hemodialysis postoperatively or low volume peritoneal dialysis to optimize the metabolic state.

Adult↗

Biosynthesis and assembly of the proton-translocating adenosine triphosphatase complex from chloroplasts.

The H(+)-translocating ATPase complex of chloroplasts consists of at least eight nonidentical subunits. Five of these (alpha, beta, gamma, delta, and epsilon subunits) collectively constitute the globular extramembranous CF(1) portion of the complex. The remaining three subunits (I-III) represent the membrane-embedded portion. Biosynthesis and assembly of these subunits were studied by pulse-labeling isolated spinach chloroplasts in the presence of cycloheximide or chloramphenicol and by translating total leaf RNA in a rabbit reticulocyte system. The labeled products were analyzed by immunoprecipitation with subunit-specific antisera or by isolating the entire H(+)-translocating ATPase complex in a nearly pure state. We found that chloroplasts synthesize the alpha, beta, gamma, and epsilon subunits of CF(1), the membrane-embedded subunit I, and probably also the membrane-embedded subunit III. The delta subunit (and probably also subunit II) are imported from the cytoplasm via larger precursor forms. After isolated chloroplasts are labeled in the presence of cycloheximide, the chloroplast-made H(+)-ATPase subunits are assembled into a complex that is indistinguishable from the authentic H(+)-ATPase complex. This assembly indicates that isolated chloroplasts contain excess pools of the cytoplasmically made subunits.

Journal Article↗

Renal gallium accumulation in rats with antibiotic-induced nephritis: clinical implications. Concise communication.

To determine the effect of antibiotic-induced nephrotoxicity on the renal accumulation of gallium, groups of ten Sprague-Dawley rats were given intraperitoneal injections of gentamycin, amphotericin, or neomycin for a period of 16--21 days. In all cases, mild to moderate nephrotoxicity was documented by one or more of the following parameters: serum creatinine, renal weight, urine volume (renal concentrating ability), light microscopy, and electron microscopy. In none of these cases was the renal accumulation of gallium increased over control values. Consequently, diffuse renal accumulation of gallium in patients with subclinical or mild nephrotoxicity is unlikely to be related to short-term treatment with aminoglycosides or amphotericin. In such cases, the physician should seek some other clinical explanation, such as infection.

Amphotericin B↗

Diary of a retread.

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Attitude of Health Personnel↗

Partial resolution of the enzymes catalyzing photophosphorylation. XV. Approaches to the active site of coupling factor I.

1. Prolonged treatment of coupling factor I (CF1) from spinach chloroplasts with trypsin free of chymotrypsin yielded an active ATPase. The isolated preparation showed only two polypeptide chains (mol wt 55,000 to 60,000) on acrylamide gels run in the presence of sodium dodecyl sulfate. The three smaller subunits of CF1 were not detectable. The preparation no longer served as a coupling factor for photophosphorylation in either EDTA- or silicotungstate-treated chloroplasts. 2. An antiserum prepared against coupling factor I from chloroplasts inhibited the ATPase activity of the trypsin-treated CF1. In contrast, antisera prepared against the two individual (denatured) subunits did not inhibit the ATPase activity when tested either alone or together, although each interacted with the trypsin-treated protein, forming precipitin lines in Ouchterlony plates. 3. The trypsin-treated enzyme was still cold-labile, showing that the three smaller subunits are not required for this property. However, the enzyme was no longer sensitive to the natural inhibitor protein which is one of its subunits (subunit epislon), but was still sensitive to inhibition by the flavonoid quercetin. 4. Two equivalents of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole were sufficient to inhibit about 80% of the ATPase activity of the coupling factor, irrespective of whether it contained two of five subunits. The inhibition was completely reversed by dithiothreitol. 5. Triated 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole was prepared. Treatment of the coupling factor with this tritium-labeled inhibitor followed by electrophoresis on acrylamide gels revealed that most of the radioactivity was incorporated into the beta subunit of the enzyme (molecular weight 56,000).

Adenosine Triphosphatases↗

The press and us.

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Health Education↗