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Pancreas-specific protein (PASP) was compared with serum amylase in 95 episodes of acute pancreatitis with the diagnoses supported by elevated amylase levels. The etiology was typical for Scandinavian countries, with alcohol as the predominant factor, followed by cholelithiasis. PASP values were clearly raised in all patients, except in three cases found to have high salivary-type amylase levels, and one patient with recurrent alcohol pancreatitis. The rise of PASP levels were in general more pronounced than the corresponding amylase elevations, especially in severe pancreatitis. The elevations were generally parallel for the two analytes, but in 41% of the cases PASP levels remained elevated 2-11 days longer than the corresponding amylase levels. PASP was, however, eliminated from the circulation at a rate comparable to that of amylase. The serum range of PASP for 259 healthy subjects was 15-111 micrograms/L with 95% of the values within 16-98 micrograms/L. The upper reference level was set at 100 micrograms/L. PASP levels were also determined for 291 patients with disorders other than acute pancreatitis. Serum levels in patients with renal insufficiency (n = 12), primary biliary cirrhosis (n = 9), and diabetes mellitus (n = 17) were equal to those in healthy subjects. Eight patients of 173 with acute abdominal disorders and no evidence of pancreatitis had elevated PASP levels as well as 4 patients with prostatic carcinoma (n = 28) and 2 patients with benign prostatic hyperplasia (n = 16). PASP values were low in chronic painful pancreatitis (n = 15) and pancreatic cancer (n = 11).

L'isopropyl-4 anisole est traite a l'aide de l'acide trifluoroacetique deuterie. En plus de l'echange d'hydrogene aromatique attendu, les hydrogenes methyliques du groupe isopropyl sont echanges. La cinetique et le mecanisme de cette derniere reaction sont etudies

A previously unknown major protein in human pancreatic cytosol has been purified and partly characterized. The protein, designated pancreas specific protein (PASP), has a molecular weight of 44,500 and a pI of 6.9. A two-dimensional gel separation technique revealed the protein to be specific for normal pancreatic tissue. Antibodies against PASP were raised in rabbits and a radioimmunoassay was developed for the quantitation of this protein. The following concentrations of PASP (mg/kg wet weight) were found in human tissues: normal pancreas 100-1,000; pancreatic carcinoma 0.1-20; prostate 0.5-5; and 13 other tissues less than 0.5. The levels of PASP in peripheral serum were less than 0.1 mg/L in normal subjects, 0.7-3 mg/L in cases of acute pancreatitis, and less than 0.1 mg/L in cases of pancreatic carcinoma, prostatic diseases, and other abdominal diseases investigated. The high tissue specificity and the specific elevation of serum PASP levels in acute pancreatitis may indicate a use of this protein as a marker of this pancreatic condition.

The steroid binding properties of the human pancreatic estrogen binding protein (hEBP) in cytosol were studied by equilibrium dialysis. A high ligand specificity of the protein was revealed. hEBP in cytosol binds unconjugated steroid estrogens with a medium affinity (Kd = 10−7M) but does not bind conjugated estrogens or unconjugated androgens, gestagens, glucocorticoids or cholesterol. Quantitation of hEBP by radioimmunoassay in subcellular fractions of human pancreatic tissue indicated that the protein is translocated into different subcellular compartments. Duodenal juice taken from patients following stimulation of pancreatic secretion by food ingestion (Lund's test) showed high hEBP concentrations, and the levels of hEBP changed concomitantly with the levels of pancreatic isoamylase, indicating that hEBP secretion was stimulated by food ingestion. The levels of hEBP in peripheral serum from healthy subjects showed no sex difference, but were positively correlated to age. Highly elevated (10–20-fold) hEBP levels were found in serum from patients wih acute pancreatitis, while normal serum hEBP values were found in other abdominal diseases. It is speculated that hEBP might have a specific role in the transport of estrogens from the peripheral circulation via the pancreas to the duodenum. The elevated hEBP levels in patients with acute pancreatitis indicate that this protein may be used as a marker of cellular damage in the pancreas.

A radioimmunoassay for quantitation of the human pancreatic estrogen binding protein (hEBP) was developed using polyclonal rabbit hEBP antiserum and iodinated purified hEBP. Parallel dose-response curves were obtained when serial dilutions of human serum and of cytosols obtained from human pancreas, prostate and colon were analyzed simultaneously with serial dilutions of purified hEBP standard. Very high levels of hEBP (500–1000 mg/kg wet weight) were found in normal pancreas. High as well as medium levels were found in pancreatic carcinoma tissue and medium values (0.1–1 mg/kg wet weight) in prostate, colon and ovarian tissue. Other tissues and serum from healthy volunteers showed low values, usually below 0.1 mg/kg. When serial dilutions of rat pancreatic cytosol were analyzed in the hEBP assay, [ 125 I]hEBP was displaced by the rat preparation, but the dose-response curves were not parallel to the standard curves, indicating similarity but non-identity between the estrogen binding proteins in human and in rat pancreas.

The peripheral serum levels of FSH, LH, testosterone, 5α-dihydrotestosterone, 4-androstene-3,17-dione and total oestrone (sum of free + conjugated oestrone, mainly oestrone sulphate) were determined in two groups of healthy males aged 40–54 and 58–79 years respectively. The mean level of FSH was higher in the older group (P < 0.05) while no significant age-dependent changes was found for LH, testosterone and 5α-dihydrotestosterone (P < 0.9, < 0.4 and < 0.1 respectively). The levels of 4-androstene-3,17-dione and total oestrone were significantly (P < 0.01) lower in the older group. The results supports the hypothesis concerning an age-dependent change in the sulphokinase/sulphatase balance and also indicate a shift in the biosynthetic process in the aging adrenal.

A study was made of the effects of some agents on the stability of unphosphorylated pyruvate kinase type L, the enzyme phosphorylated with cyclic 3',5'-AMP-stimulated protein kinase and the subtilisin-modified enzyme form from which the phosphorylatable site had been removed. The phosphorylated pyruvate kinase was found to be the most labile of the enzyme forms at high temperature and in the presence of urea. The circular dichroism spectrum of the phosphorylated enzyme also differed from that of the unphosphorylated and proteolytically modified forms. All three forms of the enzyme showed a high degree of stability over a wide pH range. The unphosphorylated enzyme seemed, however, to be the most sensitive to differences in pH. Only 10% of its maximal activity remained after incubation at pH 10 and 30 degrees C for 30 min, compared with 30% and 75% for the phosphorylated and proteolytically modified forms of the enzyme, respectively. Of the three enzyme forms tested the subtilisin-modified pyruvate kinase was most rapidly inactivated by trypsin. These results taken together suggest that the phosphorylated enzyme has a less ordered structure than the other two enzyme forms studied.

Preparation par cyclisation d'hydroxyacides (catalyse acide) ou de thioglycolate de β-halogenoethyle (catalyse basique); cinetique de l'hydrolyse des oxathianne-1,4ones-2

Etudes theoriques relatives a une reaction d'electrode A±e⇄B, suivie par des reactions homogenes de B

Pancreas-specific protein (PASP) is a recently isolated and partially characterized major protein in the human pancreas. It has not been described previously. Serum levels of PASP and amylase were analyzed in 21 patients subjected to combined renal and segmental pancreatic transplantation with both organs obtained from the same donor and in eight kidney transplant patients. In the pancreas transplant patients, PASP and amylase levels were elevated in episodes of graft pancreatitis. With chronic graft rejection, PASP rose to high levels long before other indications. In episodes of renal rejection, the levels of PASP, but not always of amylase, were elevated on several occasions. They decreased after antirejection therapy. This may indicate accompanying pancreatic graft rejection. PASP and amylase levels were stable in kidney transplant patients and were not affected by serum creatinine levels, renal rejection, or antirejection therapy. The results support earlier observations that renal rejection in combined pancreas and renal transplant patients may or may not be accompanied by a rejection process in the pancreatic graft. PASP may be the means by which to tell when the pancreatic graft is involved.

Stereochimie du transfert de proton-1,3 reversible du phenyl-3 o-tolyl-1 cyclohexene au phenyl-1 o-tolyl-3 cyclohexene en presence d'octahydro-1,2,3,4,4a,5,6,7 naphtyridine-1,8

Phospholipids which do not contain choline were found to solubilize Ni(II) in the chloroform phase resulting from the Folch extraction procedure. On the basis of this phenomenon a radioactive assay for such phospholipids was developed using 63Ni(II). This assay can be made rather sensitive by scaling down and can be performed relatively rapidly. The disadvantages are that it does not measure phosphatidyl chlorine or sphingomyelin and that different phospholipids bind different amounts of Ni(II). Alternatively, non-choline-containing phospholipids can be assayed colorimetrically on the basis of their ability to solubilize Cu(II) in the chloroform phase. The failure of phosphatidyl choline and sphingomyelin to bind divalent cations may be due to formation of an intramolecular salt between the negatively charged phosphate group and the positively charged nitrogen.

Synthese a partir de reactif de Grignard, par reaction avec CO 2 et le dichromate de tetrabutyl ammonium

Methoxylation electrochimique sur electrode de Pt dans le methanol-tetrafluoroborate d'ammonium, du formyl-1 prolinate de methyle. Etude de l'amidoalkylation du malonate de dimethyle et du mesitylene a l'aide du compose prepare

The urinary excretion of LH, low polar oestrogens, neutral C19 and C21 steroids was measured in normal healthy males aged 20-79 years. No significant changes could be noted for the excretion of LH, pregnanediol and 17-ketogenic steroids between 50 and 79 years. The excretion of androsterone and aeticholanolone was significantly lower in the oldest group (70-79 years). A significant drop in the excretion of DHA was noted at approx. 60 years. The excretion of low polar oestrogens remained constant from 20 to 55-59 years, but showed a highly significant (P less than 0.001) decrease at about 60 years. This drop might reflect a sudden decrease in the plasma levels of oestrone sulphate due to a decreased sulphurylating activity in the liver.

The estrogen binding protein in human pancreas has been purified from pancreatic cytosol by chromatography on Concanavalin-A-Sepharose and hydroxyl-apatite followed by ion-exchange chromatography carried out using a fast-protein liquid chromatography apparatus (FPLC). The purified protein, still able to bind labelled [3H]estradiol, appeared as one single band corresponding to 31 K in SDS-gel electrophoresis. Total amino acid analysis revealed high levels of histidine, glutamic acid and leucine. The capacity of the purified protein to bind estrogens could be increased more than 4-fold by addition of a cytosolic factor, probably being a small peptide, that is present in crude cytosol, but lost during the purification procedure. The iodinated protein does not bind to DNA-cellulose or phosphocellulose, and shows no similarities to estrogen receptor proteins.

Synthese d'[hydroxy-4' methoxy-3' phenyl]-2 dihydro-2,3 benzofurannemethanol-3 a partir de benzyloxy-2 methoxy-3 benzaldehyde et de benzyloxy-4' methoxy-3' acetophenone

L'oxydation des α-hydroxyacides conduit a des aldehydes (si la fonction alcool est secondaire) et a des cetones (si la fonction alcool est tertiaire) ayant un carbone de moins que les hydroxyacides de depart

A radioimmunoassay for a novel human pancreatic protein (pancreas-specific protein, PASP) has been developed. We studied the possibility that serum PASP levels reflect pancreas-graft rejections in human pancreas-transplant recipients. Ten patients subjected to combined pancreas-kidney transplantation and 4 patients subjected to pancreas transplantation alone were studied. Twelve kidney recipients served as control subjects. On several occasions, PASP levels were elevated at kidney rejections in patients with combined pancreas-kidney grafts and then decreased after antirejection therapy, although no other indications for concomitant pancreas-graft rejection were at hand. In the recipients of pancreas grafts alone, PASP levels increased before or at the same time as graft rejections were indicated by current methods. In two cases of chronic graft rejection, PASP rose to high levels long before hyperglycemie occurred. In the control group of kidney-graft recipients, PASP levels were stable and were not affected by high serum creatinine levels, kidneyrejection episodes, or antirejection therapy. This study indicates that PASP may be a good serum marker for pancreas-graft rejection.