Total parenteral nutrition via multilumen catheters does not increase the risk of catheter-related sepsis: a randomized, prospective study.

The purpose of this study was to determine in a randomized, prospective manner whether administration of total parenteral nutrition (TPN) via multilumen catheters increases the risk of catheter-related sepsis (CRS). All patients receiving hyperalimentation during a 24-month period were randomized to receive either a double-lumen catheter (DLC) or a triple-lumen catheter (TLC). A total of 101 catheters were placed in 79 patients, of which 49 were DLCs and 52 were TLCs. The patients with DLCs received a total of 784 days of TPN, whereas patients with TLCs received a total of 754 days of TPN. CRS was associated with one (2.0%) of the 49 DLCs vs. one (1.9%) of the 52 TLCs. In comparison, the rate of CRS associated with single-lumen catheters (historical control) at our institution was 1.4% (P > .90). We conclude that the use of multilumen catheters in TPN therapy does not result in an increased risk of CRS.

Pleural effusion as the major manifestation of actinomycosis.

Pleural effusion represents an unusual but significant manifestation of actinomycosis, as illustrated in this case presentation. The diagnosis was made after bronchoscopy and examination of bronchoalveolar fluid and culture. No parenchymal abnormality was noted on the chest film.

Synthesis of ascorbyl-2-phosphate by liver enzyme of rainbow trout Oncorhynchus mykiss.

1. Ascorbyl-2-monophosphate was enzymatically formed in the reaction mixture of L-ascorbic acid, pyrophosphate and the homogenate of rainbow trout Oncorhynchus mykiss liver. 2. The liver had the highest activity among the liver, spleen, kidney, stomach, pyloric caeca and intestine. 3. Pyrophosphate, triphosphate, ADP and ATP were good substrates as phosphoryl donors, but phosphoric acid and AMP were poor. 4. The optimum pH and temperature of AP-forming activity in the liver were around 5.0 and 30 degrees C, respectively. 5. The Km values for ascorbic acid and pyrophosphate were 370 and 83 mM, respectively.

Isolation of types I and V collagens from carp muscle.

1. The major constituent of carp intramuscular connective tissue was found to be Type I collagen. 2. A collagen homologous to Type V collagen of higher vertebrate was also isolated from carp muscle. 3. Relative portion of Type V collagen was higher in carp muscle than in mammalian muscles.

Specificity of the collagenolytic serine proteinase from the pancreas of the catfish (Parasilurus asotus).

The collagenolytic serine proteinase from the pancreas of the catfish (Parasilus asotus) had a pH optimum of 7.5 for native, reconstituted calf skin collagen fibrils. The enzyme was most stable at pH 6-9. The enzyme hydrolyzed heat-denatured collagen (gelatin), casein, hemoglobin and elastin in addition to native collagen but not virtually Tos-Arg-OEe, Bz-Tyr-OEe and Suc-(Ala)3-NA. The enzyme cleaved Leu-Gly (or Gln-Gly), Gly-Ile and Ile-Ala bonds on DNP-Pro-Leu-Gly-Ile-Ala-Gly-Arg-NH2 and DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg.

Purification and characterization of a collagenolytic serine proteinase from the catfish pancreas.

A collagenolytic enzyme was purified to homogeneity from the activated pancreatic extract of the catfish Parasilurus asotus by chromatography on DEAE-cellulose, hydroxylapatite, and Cellulofine columns. The molecular weight of the enzyme was estimated to be 29,500 by SDS-polyacrylamide gel electrophoresis. The enzyme is capable of degrading native, reconstituted calf skin collagen fibrils at pH 7.5 and 37 degrees C, and also of reducing the viscosity of native calf skin collagen at pH 7.5 and 20 degrees C. The SDS-polyacrylamide gel electrophoresis of thermally denatured enzyme-collagen reaction mixtures showed that the enzyme can cleave peptide bonds in the non-helical and triple-helical regions of the collagen. The enzyme was inhibited by DFP, PMSF, soybean trypsin inhibitor, and chicken ovoinhibitor, but not by metal-chelating reagents EDTA, EGTA, o-phenanthroline, or L-cysteine. These results indicate that the enzyme is a unique collagenolytic proteinase belonging to the group of serine proteinases and is a new member of the class of pancreatic enzymes.

Distribution of pancreatic elastase and metalloproteinase in vertebrates.

Elastase-like enzymes were detected as zymogens in all of the pancreatic extracts from the gummy shark, bullhead shark, angel shark, smooth hammerhead, bestel, rainbow trout, carp, eel, Japanese mackerel, yellowtail, sea bass, parrotfish, bullfrog, chicken, bluewhite dolphin, hog, rat, cat, and dog. The distribution of pancreatic elastase and metalloproteinase was examined on the basis of the effect of specific inhibitors on elastase like-activity in each extract. The results indicate that pancreatic elastases are present in all the species examined and pancreatic metalloproteinases are present only in the teleost fishes.

Characterization of an anionic trypsin from the eel (Anguilla japonica).

An enzyme, isolated from the pancreas of the eel Anguilla japonica and designated as anionic trypsin 1, had a molecular weight of 26,000 and an isoelectric point of 5.5. The amino acid composition of the enzyme was similar to that of bovine cationic trypsin as well as anionic trypsins from other species of fish. The enzyme was stable at pH 6 to 9 in the presence of calcium ions. Km and kcat values of the enzyme for N-tosyl-L-arginine methyl ester and N-tosyl-L-lysine methyl ester were quite similar to those of catfish anionic and bovine cationic trypsins.

Purification and some properties of two anionic trypsins from the eel (Anguilla japonica).

Two anionic enzymes, designated as trypsins 1 and 2, were purified from the pancreas of the eel Anguilla japonica by DEAE-cellulose column chromatography and Sephadex G-75 gel filtration. The final preparation of trypsin 1 was homogeneous but that of trypsin 2 still contained impurities. Both enzymes had similar pH optima of near 8.3 for the hydrolysis of N-tosyl-L-arginine methyl ester. Trypsin 1 was stabilized by calcium ions but the stability of trypsin 2 was not affected by calcium ions. Both enzymes were inhibited by typical trypsin inhibitors including serine proteinase inhibitors.

Purification and characterization of a new metalloproteinase with elastolytic activity from the catfish pancreas.

An elastolytic enzyme was purified to homogeneity from the pancreas of the catfish Parasilurus asotus by chromatography on CM-cellulose column and affinity chromatography on (Ala)3-CH-Sepharose 4B column. The molecular weight of the enzyme was estimated to be 24 000 by SDS-polyacrylamide gel electrophoresis. The enzyme had elastolytic activity as well as activity toward Suc-(Ala)3-NA. The enzyme was inhibited by EDTA, EGTA, o-phenanthroline, dithiothreitol, and cysteine, but not by the serine proteinase inhibitors iPr2P-F and PhCH2SO2F. In addition, the enzyme was found to require Zn2+ for activity. These results indicate that the catfish enzyme belongs to the group of metalloproteinases and that it is a new type of pancreatic enzyme, unlike the pancreatic elastases which are serine proteinases.

Enzymatic characterization of anionic trypsin of the catfish (Parasilurus asotus).

An anionic trypsin, isolated from the pancreatic extract of the catfish (Parasilurus asotus), had a pH optimum of 8.3 for the hydrolysis of N-tosyl-L-arginine methyl ester. The enzyme was most stable at pH 6.0-8.5, and was stabilized by calcium ions. The enzyme was inhibited by typical trypsin inhibitors including some serine proteinase inhibitors. Km and kcat values of the enzyme for N-tosyl-L-arginine methyl ester and N-tosyl-L-lysine methyl ester were quite similar to those of bovine cationic trypsin.