Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: HUMANGGP:021525 (albumin)
 60,984 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protease activity was detected in membranes of human bovine erythrocytes prepared by the conventional procedures which include washing and removal of the "buffy layer". The enzyme was extracted by 0.75 M KCNS or (NH4)2SO4 and was activated by 0.4 to 0.5 M of the same salts. Colored, particulate hide powder-azure, membrane fractions and soluble proteins such as hemoglobin, casein or albumin were susceptible to hydrolysis by the membraneous protease. Partial purification of the enzyme was accomplished through disc-gel electrophoresis on polyacrylamide in the presence of 0.25% positively charged detergents like cetyltrimethylammonium bromide. An alkaline protease (pH 7.4) with properties similar to those of the erythrocyte enzyme was found in leucocytes. The similarity between the properties of the leucocytic and erythrocytic proteases and the correlation of the activity in erythrocyte membranes with content of white cells in these preparations, suggest that enzymatic activities in the contaminating leucocytes are responsible for the activity of membraneous proteases in erythrocytes.
Biochim Biophys Acta 1975 Dec 16
PMID:Membrane-bound enzymes. III. Protease activity in leucocytes in relation to erythrocyte membranes. 0 92

The solubility of triclinic calcium pyrophosphate dihydrate (CPPD) crystals was measured under varying conditions using 45Ca-labeled crystals, expressing solubility as micromoles per liter of 45Ca in solution. In a 0.1-M Tris-HC1 buffer pH 7.4, the solubility of accurately sized CPPD crystals (37-20mum) was 60muM with maximal solubility being attained after about 8 h incubation at 37degreeC. Reduction in crystal size, decrease in pH, increase in ionic strength, Mg++, citrate, and albumin all increased solubility. The most marked effects on solubility occurred when changing the calcium concentration or by enzymatic hydrolysis of inoganic pyrophosphate to orthophosphate. It was found that decreasing the ionized calcium level below 5 mg/100 ml resulted in a progressive enhancement of solubility. The observed solubility-enhancing effects of albumin could be explained solely on its calcium-binding ability and thereby, altered ionized calcium level. Diffusible calcium in synovial fluid was only 40% of the total calcium concentration, which means most joint fluids are normally near the critical concentration of 5 mg/100 ml of ionized calcium, below which solubility is enhanced. During surgery, especially parathyroidectomy, calcium levels fall, favoring dissolution of CPPD crystals. We speculate that the slight decrease in crystal size during dissolution frees them from their cartilaginous mold, resulting in a dose-dependent inflammatory reaction as they are "shed" into the joint space. Crystal shedding may be reinforced by the modest fall in joint fluid pH accompanying the inflammatory response.
J Clin Invest 1975 Dec
PMID:Factors affecting the solubility of calcium pyrophosphate dihydrate crystals. 0 Apr 23

As shown previously, proteinases frequently associated with plasma albumin samples catalyze a very limited and specific cleavage of the albumin molecule when it exists in the F conformational state near pH 3.7. The primary proteolytic product, BPA, has a molecular weight similar to or identical with that of the parent protein but yields two large fragments of molecular weight approximately 46000 and 23000 on reduction. Evidence is presented here that cleavage occurs within the disulfide loop between Cys390 and Cys434 with no detectable loss of small peptides, the amino acid composition of BPA being identical with that of the parent protein within experimental error. Cleavage exposes a new amino-terminal phenylalanine residue and may occur at the Glx392-Phe393 bond although the possibility exists that it occurs at another X-Phe bond in the unsequenced region of residues 400-402. The damaged protein has a somewhat altered secondary structure as judged from optical rotatory dispersion and circular dichroism measurements, probably an approximate 15% loss in helicity. The hydrodynamic volume is increased by approximately 20%. However, various physical studies indicate the tertiary structure to be strikingly similar to that of the native protein. Of most significance is the fact that the protein still undergoes the N-F and N-B transitions, although in both cases they occur at somewhat more moderate pH than in the parent protein. Moreover a sensitivity of the N-B transition to Ca2+ is still seen and binding behavior toward the dye 8-anilino-1-naphthalenesulfonic acid is essentially unaltered. The results are best understood in terms of the concept of a multidomain structure which has been suggested frequently for plasma ablumin. Bond cleavage damages one domain but leaves the overall structure essentially unaltered except for some weakening of the interaction between domains.
Biochemistry 1975 Dec 30
PMID:Conformational properties of bovine plasma albumin with a cleaved internal peptide bond. 0 Oct 86

Urinary gamma-glutamyl transpeptidase (gamma-GT) has been found to be stable when stored at room temperature and 4 degrees C. Activity is lost rapidly when urine is frozen but prior dialysis will prevent this loss. Urea is the major factor responsible for the loss of activity; albumin is protective at concentrations of 6 g/l or more. A factor of 10 000-30 000 molecular weight which will prevent the loss of urinary gamma-GT activity on freezing has been found in serum and urine; it has high potency in serum and in urine from patients with chronic renal failure, but only low potency in normal urine. Its nature is unknown but it is heat stable.
Clin Chim Acta 1975 Dec 15
PMID:A stabilising factor for gamma-glutamyl transpeptidase in urine. 0 Nov 62

1) After intraperitoneal injection of labeled CCl4, CHCl3, and halothane in mice, 14C is preferentially bound to liver endoplasmic protein and lipid. A considerable activity is also associated with mitochondrial constituents. Maximal protein binding (nmol/mg): CCl4: 2.8 (0.5 hrs); CHCl3: 11.5 (6 hrs); halothane: 5 (6 hrs). Lipid binding: CCl4: 6.4 (5 min); CHCl3: 8 (4 hrs); halothane: 13.5 (2 hrs). The form of the binding curves in microsomal and mitochondrial protein and lipid differed with the individual haloalkanes. 2) The irreversible (covalent) binding of 14C from labeled haloalkanes in anaerobic suspensions of isolated rabbit liver microsomes and NADPH after 30 min was for protein (lipid) (nmol/mg): CCl4: 15 (58); CHCl3: 3.4 (3.2); halothane: 2.3 (10); trichlorofluoromethane: 6.5 (30). Anerobic incubation favored dehalogenation, but CHCl3 metabolism and irreversible binding requires oxygen. The greatest differences in the in vitro "covalent" binding rates were observed with CHCl3 in rat, mouse, and rabbit. 3) Altered microsomal cytochrome P-450 concentrations in newborn animals, or produced by pretreatment of rats with phenobarbital, 3-methylcholanthrene (MC), or CoCl2 effected similar, but not proportional changes in the rates of irreversible protein and lipid binding. Upon addition of CCl4 the difference of light absorption of reduced liver microsomes from MC-pretreated rats containing cytochrome P-448 appeared at 452 nm. The irreversible binding rate in these microsomes was also increased. The small accleration in irreversible binding in liver microsomes from rats pretreated with isopropanol is not proportional to the high increase of CCl4 toxicity. 4) Practically no binding to added, soluble albumin or RNA was observed in microsomal incubates. However, 14C is bound to the nicotine-adenine dinucleotides of the NADPH system. All haloalkanes produced a similar increase of NADPH oxidation in incubates of rabbit liver microsomes and NADPH.
Arch Toxicol 1975 Dec 18
PMID:A comparative study on the irreversible binding of labeled halothane trichlorofluoromethane, chloroform, and carbon tetrachloride to hepatic protein and lipids in vitro and in vivo. 0 52

The existence of a clinically feasible calcium electrode makes it possible to obtain rapid, accurate levels of ionized calcium. It is now possible to study the actual ionization of calcium under normal and abnormal physiologic conditions. The present investigation was directed at changes in ionized calcium during major surgical procedures. The total series of 125 patients was divided into three groups according to the type of plasma volume expander: group 1, whole blood alone; group 2, whole blood plus exogenous albumin, and group 3, albumin alone. Ionized calcium levels dropped significantly, p less than 0.001, in all three groups. Although albumin alone produced a decrease in ionized calcium, the addition of albumin to whole blood did not result in a greater decline than that experienced with whole blood alone. Chelation with the citrate ion of bank blood preservative was the major factor responsible for the decrease in ionized calcium. There was no statistically significant relationship between the extent of the decrease, the total volume of blood, the volume of blood per kilogram of the rate of transfusion in milliliters per kilogram per minute. Although the ionized calcium level fell initially, it increased while blood administration continued. In view of these facts, it is difficult to estimate the acutal level of ionized calcium at any point during the operation. Twenty patients in the series had ionized calcium levels below 1.25 milliequivalents per liter, range of 0.51 to 1.24 milliequivalents per liter. With the possible exception of one patient, no adverse cardiovascular effects could be attributed to the low levels of ionized calcium. The results in this series confirm our previous conclusion that the administration of exogenous calcium is not necessary during massive transfusion, with the possible exception of bypass open heart procedures and exchange transfusions in children.
Surg Gynecol Obstet 1976 Dec
PMID:Factors influencing the ionization of calcium during major surgical procedures. 1 68

Local inflammation evoked in Swiss albino mice by subcutaneous injection of Celite resulted in a rise of liver tyrosine aminotransferase activity and plasma level of fibrinogen and seromucoid, while liver alanine aminotransferase activity and plasma level of fibrinogen and seromucoid, while liver alanine aminotransferase activity and the plasma level of albumin and total protein remained unaltered. By measuring the incorporation of [14C] leucine, stimulation of liver and plasms protein synthesis by Celite injection was demonstrated. Administration of D-galactosamine (2-5 mg/10 g body weight) inhibited the enhanced synthesis of liver proteins, and especially of trauma-induced synthesis of plasma fibrinogen and seromucoid. The inhibitory effect of galactosamine was most pronounced when the amino sugar was injected simultaneously with Celite and then protein synthesis was measured 6 h later. The results obtained support the idea that high doses of galactosamine inhibit transcription of trauma-inducible mRNA in the liver and thus block the acute-phase response.
Br J Exp Pathol 1976 Dec
PMID:Inhibition of the liver and plasma protein acute-phase response in mice by D-galactosamine. 1 81

The activity of gamma-glutamyl transferase (GGT, EC 2.3.2.2) in sera of 68 healthy individuals, of 38 patients receiving anti-epileptic drugs, and of 27 patients having liver parenchymal lesions, was visualized after electrophoresis on cellulose-acetate gel using the substrate gamma-L-glutamyl-p-nitroanilide as a new colour reagent. The liberated p-nitroaniline was converted in situ into a lilac-coloured product using the Bratton-Marshall reaction. In most samples two bands were demonstrated, one located between albumin and alpha1-globulin, called GGT 1, the other located in the alpha2-globulin region, GGT 2. In a few samples a third band, GGT 3, with far less activity than the other bands, occurred in the beta-globulin region. When it occurred, an increase in total GGT activity was mainly due to an increase of GGT-1 activity. The possible role of the determination of GGT-1 activity as a monitor of microsomal enzyme induction is discussed.
Clin Chim Acta 1978 Dec 15
PMID:A new procedure for the visualization of multiple forms of gamma-glutamyl transferase (GGT). Results in normals, patients receiving enzyme-inducing drugs and patients having liver parenchymal lesions. 3 92

It has been demonstrated recently that the reaction of serum samples with bromcresol green (BCG) reagent proceeds in two steps. Albumin is responsible for the immediate reaction while other serum proteins produce the slow reaction. In this paper the immediate BCG reaction has been used for the determination of urinary albumin concentration in patients with proteinuria by a slightly modified method with a primary pH adjustment of the urine and the use of a urine blank. Comparison of the immediate BCG method (y) with Laurell "rocket" technique (x) gave the following equation: y = 17.2 + 1.006x (n = 98; r = 0.99) mg/l. The coefficient of variation (within-day), C.V. (%), ranged between 0.9 and 2.7% depending on the albumin concentration. It is thus possible to carry out rapid, accurate and precise albumin determinations in urine samples using this simple method.
Clin Chim Acta 1978 Dec 15
PMID:Urinary albumin determination by the immediate bromcresol green method. 3 93

Antibodies to the nucleosidel,N(6)-ethenoadenosine have been used to localize the site of adenylylation of the glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2] of Escherichia coli. Antibodies were induced in rabbits by injection of a bovine albumin-ethenoadenosine conjugate. The resulting antisera strongly bound ethenoadenosine, its 5'-nucleotide, or protein conjugates of the nucleoside; little or no crossreaction was seen to adenosine, AMP, or the protein carrier. Ethenoadenylylated glutamine synthetase was prepared by modification of the enzyme by the E. coli adenylyltransferase, using etheno-ATP as a substrate. The ethenoadenylylated glutamine synthetase was precipitated by antibodies to ethenoadenosine in conjunction with goat anti-rabbit gamma globulin. Electron micrographs of reaction mixtures of ethenoadenylylated glutamine synthetase and anti-ethenoadenosine showed individual enzyme molecules complexed with one or more antibodies and pairs of enzyme molecules crosslinked by a single antibody. The approximate site of adenylylation was located from the apparent area of contact between enzyme and antibody. We conclude that the adenylylation sites are on the periphery of the bilayered hexagonal disc, offset by 15 +/- 10 degrees from the 2-fold axis of symmetry through a vertex of the hexagon and 20 +/- 10 A from the plane between the layers of the disc.
Proc Natl Acad Sci U S A 1978 Dec
PMID:Localization of the site of adenylylation of glutamine synthetase by electron microscopy of an enzyme-antibody complex. 3 36


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