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Biomedical subjects

S Sahu

Publications and source records attributed to S Sahu.

At least 37 records · Page 2Linked to original sources
PubMed1981

Coping with perinatal death.

After the death of a newborn baby, parents experience a grieving process much the same as any other form of grief. This process should be recognized as a normal event. It may be especially traumatic when siblings must share in the process. Parents go through the various stages of grief. The health care provider should fulfill his or her role in the grieving process by recognizing the stages of grief and providing help and support to the family at appropriate times. From the time of the baby's death until many months after, health professionals should help make the grieving process more tolerable.

Death↗
PubMed1980

Biochemical studies on pulmonary response to inhalation of methylene chloride.

Biochemical response to the toxic lung damage induced by inhalation of methylene chloride was studied. Significant increases in protein, hexose, sialic acid, lactate dehydrogenase, acid and alkaline phosphatase content were observed in the cell-free lavage effluents from lungs of exposed rats compared to the control animals. This was interpreted as increased cell damage accompanied by enhanced pulmonary secretions, perhaps of glycoproteins and mucins, as a result of inhalation toxicity.

Alkaline Phosphatase↗
PubMed1979

Isolation and characterization of proteoglycans from porcine lungs.

Proteoglycans were extracted from porcine lungs with 4 M guanidinium chloride. The extract was subjected to associative density gradient centrifugation, and four equal fractions, labeled A1 through A4 from the bottom to the top of the gradient, were obtained. The pooled A1 fractions containing proteoglycan aggregates were further fractionated by dissociative density gradient centrifugation to yield four equal fractions labeled A1D1 through A1D4 from the bottom to the top of the gradient. These fractions were analyzed for their protein, uronic acid, glucosamine, galactosamine, hexose, and sialic acid content. The fraction A1D1 with the highest buoyant density had the highest content of uronic acid and galactosamine, and lowest content of protein, indicating the enrichment of proteoglycan monomers at the bottom of the dissociative density gradient. As the density of the gradient decreased, the protein, hexoses, and sialic acid content increased, whereas uronic acid and galactosamine content decreased. The amino acid analysis showed similar composition for all four fractions with aspartic acid, serine, glutamic acid, proline, glycine, alanine, valine, and leucine as the major constituent amino acids. No hydroxyproline was detected in any of the fractions. As the buoyant density of the fractions decreased, the aspartic acid content increased and glycine content decreased.

Amino Acids↗
PubMed1979

Characterization of a high-molecular-weight glycoprotein isolated from the pulmonary secretions of patients with alveolar proteinosis.

A high-molecular-weight glycoprotein was isolated, purified and partially characterized from the insoluble pulmonary secretions accumulating in lungs of patients suffering from pulmonary alveolar proteinosis. On electrophoresis in 5% polyacrylamide gel in the presence of sodium dodecyl sulphate and 2-mercaptoethanol, the purified protein gave one major band as detected by Coomassie Blue as well as with periodic acid/Schiff staining. An apparent mol.wt. of 250000 was estimated for this glycoprotein. Amino acid analysis showed that it contains hydroxyproline, and relatively high amounts of glycine, glutamic acid, aspartic acid and leucine. It contains approx. 6% hexose, 3% sialic acid and 2% glucosamine. The neutral sugars are galactose, mannose and fucose. An antiserum prepared in rabbits against this high-molecular-weight glycoprotein cross-reacted with two smaller glycoproteins (mol.wts. 62000 and 36000) isolated from the same pulmonary secretions of these patients. A complementary observation was also made when this large alveolar glycoprotein cross-reacted with an antiserum prepared in rabbits against the smaller glycoprotein (mol.wt. 36000). It appears that this high-molecular-weight glycoprotein may be the precursor of the two smaller glycoproteins present in the same diseased pulmonary secretions.

Amino Acids↗
PubMed1979

Characterization of a 130,000-dalton glycoprotein isolated from pulmonary secretions of patients with alveolar proteinosis.

A new glycoprotein with an apparent molecular weight of 130,000 was isolated, purified, and partially characterized from the pulmonary secretions which accumulate so massively in the lungs of patients suffering from pulmonary alveolar proteinosis. The amino acid analysis of the glycoprotein showed the presence of relatively high amounts of glycine, glutamic acid, aspartic acid, leucine, and valine, and small amounts of hydroxyproline, but no hydroxylysine. It contains approximately 6% hexose, 3% sialic acid, and 4% glucosamine. The neutral sugars are galactose, mannose, and fucose. This alveolar glycoprotein cross-reacted with an antiserum prepared in rabbits against a larger glycoprotein (250,000 mol wt) isolated from the same source, suggesting that the larger alveolar glycoprotein may be the precursor of the smaller one.

Amino Acid Sequence↗
PubMed1978

Hyaluronic acid in the pulmonary secretions of patients with asthma.

Hyaluronic acid was the only glycosaminoglycan found in the pulmonary secretions of patients with asthma. The compound had a hexuronate/hexosamine molar ratio of about 1:1. Glucosamine constituted over 98% of the hexosamines, the remaining being galactosamine. The compound moved as a single spot with the mobility of standard hyaluronic acid on cellulose acetate electrophoresis, and this spot disappeared after digestion with testicular hyaluronidase. Even after extensive proteolysis and purification, the compound was associated with small amounts of protein, the major amino acids of which were aspartic acid, threonine, serine, glutamic acid, glycine and valine.

Adult↗
PubMed1978

Hyaluronic acid in the pulmonary secretions of patients with alveolar proteinosis.

Hyaluronic acid was the only glycosaminoglycan found in the pulmonary secretions of patients with alveolar proteinosis. The compound gave a hexouronate/hexosamine molar ratio of about 1:1. Glucosamine constituted over 98% of the hexosamines, the remaining being galactosamine. It moved as a single spot with the mobility of standard hyaluronic acid on cellulose acetate electrophoresis, and this spot disappeared after digestion with hyaluronidase. It was associated with small amounts of proteins, the major amino acids of which are aspartic acid, glutamic acid, glycine, alanine, and leucine.

Amino Acids↗
PubMed1978

Lipid composition of sputum from patients with asthma and patients with cystic fibrosis.

Lipids from the sputum of patients with asthma and with cystic fibrosis were isolated and characterized. In both cases, lipids constituted approximately 30% of the dry material. Phosphatidlycholine was the most abundant lipid, Significant amounts of phosphatidylethanolamine and phosphatidylglycerol were present. Hexosyl ceramides, sphingomyelin, phosphatidylinositol, lysophosphatidylcholine, and lysophosphatidylethanolamine were present as minor lipid components. Apperciable quantities of neutral lipids were present, of which triglycerides and cholesterol were the main constituents. Phosphatidylcholine, sphingomyelin, and phosphatidylgycerol were highly saturated. Large amounts of phosphatidylcholine containing mostly palmitic acid, particularly in the asthmatic sputum, suggest htat this highly saturated. Large amounts of phosphatidylcholine containing mostly palmitic acid, particularly in the asthmatic sputum, suggests that this highly saturated phospholipid is synthesized in the upper airways for reasons other than its beneficial surface-active properties in the alveoli.

Adolescent↗
PubMed1977

Characterization of phospholipase A from pulmonary secretions of patients with alveolar proteinosis.

Phospholipase A2 (EC 3.1.1.4) from the insoluble pulmonary secretions that accumulate in the lungs of patients with alveolar proteinosis has been purified. The pure enzyme gives a single sharp band upon sodium dodecyl sulfate polyacrylamide gel electrophoresis. Amino acid analysis of the protein shows high content of cystine, aspartic acid, glutamic acid, serine, glycine, leucine and lysine. Only one N-terminal residue, alanine, can be detected. Gel filtration as well as sodium dodecyl sulfate polyacrylamide gel electrophoresis indicate an apparent molecular weight of 75 000 for the enzyme. The enzyme activity has a pH optimum between 7.5 and 8.5 and is stimulated by sodium deoxycholate and CaCl2.

Amino Acids↗
PubMed1977

Metabolism of arachidonic acid in rabbit alveolar macrophages.

Rabbit alveolar macrophages incorporated radioactive arachidonic acid primarily into phosphatidylcholine, phosphatidylethanolamine, sphingomyelin, and triglycerides. When these cells, so labelled, were washed and treated with polystyrene beads, there was a distinct and reproducible decrease in the radioactivity of phosphatidylcholine, phosphatidylethanolamine, and triglycerides. This decrease was accounted for by the appearance of two major prostaglandins, PGE2 and PGF2alpha, and uncharacterized hydroxy fatty acids, which may be 12-hydroxy-5,8,10,14-eicosatetraenoic acid, 5-hydroxy-6,8,11,14-eicosatetraenoic acid, and/or 8-hydroxy-9,11,14-eicosatrienoic acid.

Animals↗