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Biomedical subjects

D Gillessen

Publications and source records attributed to D Gillessen.

At least 37 records · Page 2Linked to original sources
PubMed1983

Influenza virus site recognized by a murine helper T cell specific for H1 strains. Localization to a nine amino acid sequence in the hemagglutinin molecule.

The functional helper T cell line Vir-2, derived from a PR8 (H1N1) influenza virus-immunized BALB/c mouse, proliferates in response to syngeneic antigen-presenting cells and naturally occurring strains of subtype H1 human influenza virus from 1934-1957 and 1977-1980 isolates. A conserved region of the hemagglutinin molecule around amino acid position 115 in the heavy chain (HA1) was implicated as being important in this recognition by the lack of stimulatory activity associated with a glutamic acid to lysine substitution at position 115 in the laboratory mutant RV6, derived from wild-type PR8. Characterization of the stimulatory determinant on the wild-type hemagglutinin molecule was then undertaken using cleavage products and synthetic peptides. Vir-2 cells recognized the reduced and alkylated purified HA1 of PR8 virus, and this reactivity was retained after cleavage at methionine and tryptophan residues. High-pressure liquid chromatography separation of cleavage fragments indicated that a short sequence of the HA1 containing residue 115 was being recognized. This recognition was localized to a nine amino acid segment (positions 111-119) by assaying stimulation with synthetic peptide homologues of different lengths from that region. As with native hemagglutinin, Vir-2 cells responded to active peptides when presented by H-2d but not H-2k antigen-presenting cells.

Amino Acid Sequence↗
PubMed1982

Human low-molecular-weight urinary urokinase. Partial characterization and preliminary sequence data of the two polypeptide chains.

Low-molecular-weight urokinase (molecular weight 33100) was separated by analytical and preparative isoelectric focusing into five major subforms with isoelectric points between 8.7 and 9.6. These subforms are very similar in molecular weight, specific activity, amino acid composition and content of amino sugar and their N-terminal sequence constellation is identical. Low-molecular-weight urokinase consists of two polypeptide chains connected by a single disulfide bridge. The N-terminal region of the heavy chain (calculated Mr 30700) exhibits homology within the first 46 residues analyzed, with the known primary structure of other serine proteases. The mini chain (Mr 2426), whose complete sequence was determined, consists of 21 residues which show homology with the primary structure of the C-terminal region of the plasmin heavy chain. Based on sequence data and homology criteria with serine proteases a single-chain urokinase precursor is postulated having a peptide bond constellation between heavy and light chain region compatible with the requirements for serine protease activation.

Amino Acid Sequence↗
PubMed1982

Biological and immunological properties of human gastrin I analogues.

The 15-methionine of human little gastrin I, prone to oxidation with concomitant loss of biological activity, has been replaced by leucine, norleucine and methoxinine, respectively. The resulting analogues exhibit acid secretory potencies practically undistinguishable from that of the parent hormone, whereas their immunoreactivity, as assayed with four different antisera raised against human little gastrin I, reflect to a significant extent the afforded modifications. Only [15-methoxinine]human little gastrin I retains practically the full reactivity for all antisera examined. The results suggest that this 15-methoxinine analogue is well suited for both biological and immunological studies.

Animals↗
PubMed1981

Assessment of exocrine pancreatic function by oral administration of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (Bentiromide): 5 years' clinical experience.

Exocrine pancreatic function was assessed in 588 subjects by oral administration of 1 g of the chymotrypsin-labile peptide N-benzoyl-L-tyrosyl-p-aminobenzoic acid (Bentiromide) from 1974 to 1979. The pancreatic function test (PFT) was performed in 126 controls, 217 patients with pancreatic diseases, 196 patients with various non-pancreatic gastrointestinal disease, 18 patients with renal disease and 31 patients with various other diagnoses. In 62 of 72 patients (86 per cent) with chronic pancreatitis and in 19 of 25 (76 per cent) with pancreatic carcinoma, the excretion of p-aminobenzoic acid (PABA) in the urine was significantly less than in the controls. In contrast, 328 of 353 controls and patients with non-pancreatic diseases (93 per cent) had PABA excretion within normal limits. The sensitivity and specificity of the Bentiromide-test observed in this study is sufficient to detect moderate to severe disturbances of pancreatic exocrine function. The PFT has proved to be an easy and reliable screening test for pancreatic exocrine function in ambulatory as well as in hospitalized patients.

4-Aminobenzoic Acid↗
PubMed1981

Comparison of the primary structure of the N-terminal CNBr fragments of human, bovine and porcine plasminogen.

The primary structures of the N-terminal CNBr fragment of human, bovine and porcine plasminogen were determined by automated Edman degradation in a combination of liquid and solid-phase techniques and also by applying the carboxypeptidase method. The comparison of the fragments showed three highly homologous and two variable regions. The heptapeptide sequence responsible for intramolecular interaction is preserved in a conservative region, whereas the sequence of the acidic loop varies considerably between the species. In the bovine and porcine fragments 18 of the 57 residues are exchanged when compared with the fragment of human plasminogen, whereas only 11 exchanges occur between the two fragments of animal origin.

Amino Acid Sequence↗
PubMed1981

The release of pancreatic polypeptide by CCK-octapeptide and some analogues in the dog.

In dogs with gastric and pancreatic Thomas fistulas the effect of different cholecystokinin-like peptides upon pancreatic polypeptide (PP) release was studied in three ways: (a) Plasma PP concentrations were determined by radioimmunoassay in response to 135 pmol/kg/h of the synthetic C-terminal octapeptide of cholecystokinin (CCK-OP) (A), of three of its analogues (B, C, D) where methionine has been replaced by methoxinine, and in response to 45 pmol/kg/h of caerulein. The greatest rise in plasma PP concentration expressed as delta PP was achieved with caerulein (327 +/- 37 pM), when taking into account the threefold smaller dose used, followed by CCK-OP (536 +/- 67 pM) and analogues B (343 +/- 51 pM), C (87 +/- 46 pM), and D (32 +/- 15 pM). The order of potency with respect to stimulation of exocrine pancreatic secretion was the same: E and A precede B, C, and D. delta PP correlated linearly with the pancreatic protein output (r = 0.98, p less than 0.01). (b) CCK-OP was infused in four doses of 35, 70, 135, and 270 pmol/kg/h, and plasma PP concentrations and exocrine pancreatic secretion were monitored. The correlation between pancreatic protein output and delta PP was very close (r = 0.98, p less than 0.01). (c) Atropine sulfate (0.1 mg/kg, i.v.) reduced the PP response to the 135 pmol/kg/h dose of CCK-OP by 61%. We conclude from this that CCK-OP and related peptides do release PP and that their effect on exocrine pancreatic secretion is closely correlated with their PP-releasing capacity. The PP release may therefore be used as an indicator of the CCK-like activity of CCK fragments and analogues. CCK-OP may well represent one of the humoral stimulatory factors contributing to the release of PP, but this action appears to depend on a cholinergic background.

Animals↗
PubMed1980

alpha 1-Microglobulin from normal and pathological urines.

alpha 1-Microglobulin was purified from normal and pathological urines. Significant differences were found in the amino acid compositions of the alpha 1-microglobulin isolated from these two sources. In addition electrofocusing of alpha 1-microglobulin from normal urine gave rise to two peaks of equal intensity with rather acidic isoelectric points (3.8 and 4.2), whilst alpha 1-microglobulin from pathological urine showed two peaks in a 1:5 ratio with less acidic isoelectric points (4.2 and 4.7). Further charge heterogeneity was also observed in the second peaks from both sources. The sugar compositions were also established, as well as the N-terminal sequences of the alpha 1-microglobulin of both peaks isolated from normal and pathological urines.

Alpha-Globulins↗
PubMed1980

Biological activity of the C-terminal octapeptide of cholecystokinin, of three of its analogues and of caerulein in the dog.

Dose-response curves of the C-terminal octapeptide (CCK-8) of cholecystokinin, of 3 of its methoxinine analogues, and of caerulein for various variables of exocrine pancreatic secretion have been established in conscious dogs. The following relative potencies were calculated for the protein secretion activity of CCK-8 (100%), [Mox3]-CCK-8 (52%), [Mox6]-CCK-8 (27%), [Mox3,Mox6]-CCK-8 (19%) and caerulein (178%).

Animals↗
PubMed1980

Localization of individual lysine-binding regions in human plasminogen and investigations on their complex-forming properties.

After partial digestion of human plasminogen with elastase, followed by chymotryptic cleavage of one of the fragments produced, two polypeptides with molecular weights of approximately 10 000 and with lysine-binding sites still intact were isolated by means of affinity chromatography and gel filtration. One fragment, which was completely sequenced (88 residues), was identified as the fourth kringle, whereas the other, according to partial sequence analysis represented the first kringle. Equilibrium dialysis against 6-aminohexanoic and yielded for the first kringle one high-affinity binding site (Ka = 60 mM-1) and for the fourth kringle one single low-affinity binding site (Ka = 28 mM-1). Moreover, interactions were detected between the first kringle and the N-terminal CNBr fragment of plasminogen and also fibrin. In these cases an additional lysine-binding site, though of low affinity, appears to be involved. Thus, the first kringle seems to play important roles, structurally by contributing to the maintenance of a compact structure of plasminogen through an intramolecular interaction with its N-terminal polypeptide region, and functionally by increasing the fibrin affinity of Lys-plasminogen (plasminogen lacking the first 76 residues) and plasmin.

Amino Acid Sequence↗
PubMed1979

Syntheses and biological activities of methoxinine-analogues of the C-terminal octapeptide of cholecystokinin-pancreozymin.

The C-terminal octapeptide of cholecystokinin-pancreozymin and its analogues in which the methionine residues were successively replaced by methoxinine have been synthesized. When these analogues were tested for their gallbladder-contraction activity in an in vitro system the following relative potencies were observed: [Mox3]-CCK-PZ 8 (95%), [Mox6]-CCK-PZ 8 (5%) and [Mox3, Mox6]-CCK-PZ 8 (2%).

Amino Acid Sequence↗
PubMed1976

Investigations on the primary structure of human plasminogen. Further evidence for sequence homology.

NH2-Terminal sequences were determined by the automated Edman method in four fragments which were isolated from a mixture of fragments obtained by CNBr cleavage of human plasminogen. One of the fragments whose sequence was determined over the first 31 residues shows sequence homologies with the fragment that forms the linkage between the plasmin chains and also with the non-thrombin part of prothrombin.

Amino Acid Sequence↗