Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eleven diabetics (eight with type I diabetes) aged 20 to 45 years underwent salivary investigations on two occasions, one to five months apart, during different metabolic control. Stimulated salivary flow rate showed a great inter-individual variation, and was not changed by improved metabolic control. Salivary glucose concentration was lower during the period of better metabolic control. In stimulated parotid saliva a positive correlation between glucose levels in saliva and blood was seen. A blood glucose threshold for glucose excretion at about 10-15 mmol/L might be present. There were no significant differences in pH, buffering capacity, total amount of protein, amylase, lysozyme, peroxidase or electrolytes (Na+, K+, Ca2+, PO42- and Mg2+) in the saliva between the two occasions of different metabolic control. In conclusion, the degree of diabetic metabolic control does not seem to be of major importance for salivary flow rate or composition in diabetics except for the salivary glucose concentration.
...
PMID:Salivary flow rate and salivary glucose concentration in patients with diabetes mellitus influence of severity of diabetes. 367 66

The excretory duct of the lacrimal gland of rabbits and guinea pigs was cannulated in situ for collection of pure lacrimal gland fluid, not contaminated by secretions from the Harderian gland or contributions of desquamating cells of the conjunctival and corneal epithelium. Tears as well as lacrimal gland fluid of both species showed a species-specific and molecular weight-dependent pattern after sodium dodecylsulphate-polyacrylamide (SDS-PAA) gradient slab gel electrophoresis. The most striking difference in both species was a protein corresponding to serum albumin present in tears and almost lacking in lacrimal gland fluid. Likewise, a variety of enzymes, total protein and PGE2 were measured in tears and lacrimal gland fluid. For rabbit tears the lacrimal gland is the primary tissue source of lysozyme (LZM), beta-hexosaminidase (beta-hex), angiotensin-converting enzyme (ACE), plasminogen activator (PA) and total protein, while lactate dehydrogenase (LDH) and the greater part of prostaglandin E2 (PGE2) are present in rabbit tears mainly as products from other ocular tissue sources. In guinea pig tears peroxidase (POD), ACE, PA and less PGE2 are exceted by the lacrimal gland, amylase (AMY), LDH and a substantial amount of PGE2 are added to the guinea pig tears by other ocular tissue sources. Beta-hex and total protein are released from the lacrimal gland and from other ocular tissue sources as well.
...
PMID:Comparison of tears and lacrimal gland fluid in the rabbit and guinea pig. 386 12

Both resting and paraffin-stimulated whole saliva were studied in 25 patients with fissured tongue and in their age and sex-matched healthy controls. The groups did not differ in dental or periodontal health. No significant differences were found between the groups in the salivary secretion rate, pH and buffer capacity, or in the frequency of lactobacilli and yeasts in saliva samples and scrapings from tongue surface. In patients with fissured tongue, unstimulated whole saliva displayed significantly elevated levels of sodium, lysozyme, myeloperoxidase and all immunoglobulins (isotypes A, G and M) when compared with the controls. These changes most likely reflect the inflammation frequently seen in the biopsies of fissured tongue. No differences between the groups existed in the amounts of salivary potassium, calcium, inorganic phosphate, amylase and total protein. Our study shows that in patients with fissured tongue the salivary secretion and composition are normal. However, components from plasma and inflammatory cells are diagnostically elevated in the whole saliva samples of patients with fissured tongue when compared with the healthy controls.
...
PMID:Changes in composition of whole saliva in patients with fissured tongue. 386 14

Human milk has many unique properties that benefit the breast-fed infant. Several of these properties reside in the protein fraction of human milk; eg, host defense factors (such as immunoglobulins, lysozyme, and lactoferrin), digestive enzymes (lipases, proteases, amylase), specific binding proteins, and growth factors. Increased knowledge of human milk proteins and their biochemistry will aid our understanding of their physiological significance in the infant.
...
PMID:Biochemistry and physiological function of human milk proteins. 393 58

We reported in a previous paper that the pattern of change in the lysozyme content of normal amniotic fluid during pregnancy resembles indices of fetal maturity such as L/S ratio, creatinine concentration and amylase activity. In order to clarify the origin of amniotic fluid lysozyme and to determine whether or not the amniotic fluid lysozyme concentration indicates the maturity of some specific fetal organ, we measured the lysozyme content of samples of materials considered to be possible sources of amniotic fluid lysozyme. These materials were amnion and--taken immediately after birth--saliva, urine and cord serum. Lysozyme content was 36.5 +/- 6.7 micrograms/ml in the saliva samples, 5.3 +/- 0.9 micrograms/ml in the urine samples, and 17.4 +/- 4.4 micrograms/ml in the cord serum samples. It is unclear, however, which material was the most important source of amniotic fluid lysozyme. The results suggested that homogenized amnion samples contained lysozyme, although the content was low, and that amnion tissue produced lysozyme in vivo. Lysozyme is an enzyme found in the lysozymes of cells. The results of this study provide evidence that amniotic fluid lysozyme originates from many sources.
...
PMID:Origin of lysozyme in amniotic fluid. 397 51

Elimination of low molecular weight proteins during sequential ultrafiltration/dialysis was studied in 29 uremic patients. Beta-2-microglobulin, retinol binding protein, free light chains lambda and kappa, Zn-alpha-2-glycoprotein, hemopexin, prealbumin, hemoglobin, albumin, acid alpha-1-glycoprotein, haptoglobin, alpha-1-antichymotrypsin, ribonuclease, lysozyme, amylase, non-specific esterase, and proteolytic activity were detected in all ultrafiltrates tested. The level of total protein and ribonuclease was determined in 36 crude ultrafiltrates from 23 patients. Concentrated ultrafiltrates were used to quantitate retinol binding protein, prealbumin, albumin, lysozyme, and amylase. Other proteins identified in the ultrafiltrates are present in trace amounts. The question was discussed whether ++inextensive but systematic loss of proteins during hemofiltration in chronic RDT might be the cause of patient homeostasis disturbances.
...
PMID:Detection of plasma proteins during sequential ultrafiltration/dialysis. 406 85

The peroxidase of human parotid saliva has been purified by concentration, gel filtration on Sephadex G-200, and ion exchange chromatography on Amberlite CG-50. The purified product was devoid of amylase activity, lysozyme activity, and immunoglobulin A (IgA). However, it had an inhibitory effect on the growth of Lactobacillus acidophilus in complete growth medium and on lysine accumulation by L. acidophilus in a buffer-glucose medium, when combined with thiocyanate ions. The concentrations of peroxidase and thiocyanate ions employed were within the range found in saliva. The fractions which contained IgA did not have an anti-bacterial effect on L. acidophilus under the conditions employed. Parotid saliva also contained low molecular weight inhibitors of peroxidase activity. These studies support the involvement of the salivary peroxidase in an antibacterial system in saliva.
...
PMID:Antibacterial activity of the purified peroxidase from human parotid saliva. 418 66

This paper reports on the concentration of total protein, reducing sugar, and various enzymes in uterine flushings obtained from 17 mature, regularly cyclic baboons and stored at -10 degrees C until required. It was found that the levels of total protein and reducing sugar was high at both the early proliferative and late secretory stages of the menstru al cycle and fell to their lowest levels in the early secretory phase. When an IUD was in situ, higher levels of these 2 constituents occurred. Of the enzymes measured in the early secretory phase, only hemoglobinase was significantly elevated in the presence of an IUD. Trypsin, chymotrypsin, lysozyme, amylase, and phosphatase were usually detectable in the flushes, but none was significantly altered by the device. The possible biologic implications of these findings are discussed.
...
PMID:Studies on uterine flushings in the baboon. II. The effect of an intrauterine contraceptive device on certain biochemical parameters. 435 88

Four proteins, which have been designated A, B, C and D, have been purified from human parotid saliva. These proteins are the major constituents of parotid saliva which migrate rapidly to the anode in polyacrylamide electrophoresis at pH9.5. Gel filtration and polyacrylamide electrophoresis were employed in the purification procedures. After purification all four preparations were tested for homogeneity by electrophoresis at pH2.8 and 9.5, by isoelectric focusing in the pH range 3-10, by immunodiffusion, and by sedimentation in the analytical ultracentrifuge. None of the proteins showed significant activity in assays for amylase, acid and alkaline phosphatase, protease, lysozyme, ribonuclease, peroxidase, beta-glucuronidase, beta-galactosidase, iron-binding activity and esterase. No cross-reactions were detected with antisera specific for lactoferrin and 15 serum proteins. All four proteins were rich in glutamic acid, proline and glycine and were lacking completely the sulphur-containing amino acids. Proteins A and C contained no threonine or tyrosine. Carbohydrate could be demonstrated only in protein A at a concentration of 4% of the total protein.
...
PMID:Purification and partial characterization of four proteins from human parotid saliva. 500 93

Extracts of Acanthamoeba castellanii (Neff) contain alpha- and beta-glucosidase, beta-galactosidase, beta-N-acetylglucosaminidase, amylase, and peptidase. All of these activities are optimal between pH 3 and 4. These extracts also were found to clarify suspensions of cell walls from nine different gram-positive bacteria, including Micrococcus lysodeikticus. The pH optimum for the lytic activity was between 3 and 4. The extent of lysis of the various cell walls did not correlate with the release of free amino groups and of free N-acetylated sugars from the walls during digestion with these extracts. Suspensions of cell walls of Escherichia coli (a gram-negative bacterium), Cordiceps militaris (a fungus), and Acanthamoeba cysts, as well as of colloidal chitin, were not clarified by incubation with these extracts, although reducing sugars were released from each of these materials. Exhaustive digestion of M. lysodeikticus walls by lysozyme released no free N-acetylglucosamine. The products of exhaustive digestion of this cell wall with Acanthamoeba extracts were free N-acetylglucosamine, free N-acetylmuramic acid, glycine, alanine, glutamic acid, lysine, and N-acetylmuramic acid peptide fragments. These results suggest that the amoeba extracts contain endo- and exo-hexosaminidases, in addition to beta-hexosaminidase and peptide hydrolases.
...
PMID:Effect of lytic enzymes of Acanthamoeba castellanii on bacterial cell walls. 578 74


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---