| 1. |
- Abrahamsson, Per-Anders, et al.
(author)
-
Radioimmunoassay of beta-microseminoprotein, a prostatic-secreted protein present in sera of both men and women
- 1989
-
In: Clinical Chemistry. - 0009-9147. ; 35:7, s. 1497-1503
-
Journal article (peer-reviewed)abstract
- We describe a simple radioimmunoassay of beta-microseminoprotein, one of the three most abundant secretory proteins of the prostate gland. The detection limit of the assay is 1 microgram/L, and its precision, expressed as the total coefficient of variation, is less than 10% for values between 10 and 150 micrograms/L. Using this assay, we found that beta-microseminoprotein immunoreactivity was present in sera from both sexes at about the same concentration. The protein detected had the same molecular size on gel chromatography as the protein isolated from seminal plasma, and dilution curves for the sera paralleled that for the pure protein. The findings suggest that beta-microseminoprotein is present in serum of healthy subjects of both sexes and that it originates in tissue other than the prostate gland. The range of the serum concentration was 0-10.6 micrograms/L (median 4.1) for 51 healthy adult women and 1.1-14.7 micrograms/L (median 6.2) for 35 healthy adult men not older than 40 years. In males with prostatic cancer the concentration in serum was highly variable and often greatly increased. The concentration of beta-microseminoprotein was correlated with that of creatinine in serum, suggesting that the protein is eliminated--at least partly--from the circulation by glomerular filtration. Little of the protein was present in the urine of women. In urine from men the concentration was high and variable, probably because of local contribution from the prostate gland to the urethral urine.
|
|
| 2. |
- ERIKSSON, STEN, et al.
(author)
-
Familial α1‐Antichymotrypsin Deficiency
- 1986
-
In: Acta Medica Scandinavica. - : Wiley. - 0001-6101. ; 220:5, s. 447-453
-
Journal article (peer-reviewed)abstract
- ABSTRACT We studied patients and their relatives with partial deficiency, approximately 50% of normal plasma levels, of α1‐antichymotrypsin (ACT), an acute phase reactant with anti‐cathepsin G activity. Six of eight ACT deficient individuals, over 25 years of age, had liver and three of eight lung manifestations, varying from severe disease to subtle laboratory abnormalities. The ACT of deficient individuals (who are heterozygotes for a rare gene, q=0.003) had normal crossed immunoelectrophoretic properties. The abnormal gene is inherited in an autosomal, dominant way. The results suggest that deficiency of this antiprotease, which also has immune response modulating properties, may predispose to liver and lung disease. 1986 Association for the Publication of the Journal of Internal Medicine
|
|
| 3. |
- Jeppsson, Jan olof, et al.
(author)
-
Isolation and characterization of two minor fractions of α1,-antitrypsin by high-performance liquid chromatographic chromatofocusing
- 1985
-
In: Journal of Chromatography A. - 0021-9673. ; 327, s. 173-177
-
Journal article (peer-reviewed)abstract
- α1-Antitrypsin is a glycoprotein that separates into five electrophoretic fractions, viz. M2, M4, M6, M7 and M8. Con A-Sepharose separates the protein into three fractions according to the branching degree of the three oligosaccharide chains. The Con A affinity is identical for M4 and M7 and for M6 and M8. Within each pair the proteins were isolated by rapid chromatofocusing. The M7 and M8 have the same carbohydrate structure as the major M4 and M6 respectively, but have lost the first five N-terminal amino acids (Glu-Asp-Pro-Glu-Gly) as compared to the majority of the protein.
|
|
| 4. |
- Lilja, Hans, et al.
(author)
-
Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa
- 1989
-
In: Journal of Biological Chemistry. - 0021-9258. ; 264:3, s. 900-1894
-
Journal article (peer-reviewed)abstract
- The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two additional transcripts, one seminal vesicular 2.2-kb species and one epididymal 2.0-kb species, code for related proteins that have a close structural relationship as well as antigenic epitopes in common with semenogelin. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localized to the parts of the spermatozoa involved in locomotion. The spermatozoa become progressively motile as the gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves.
|
|
| 5. |
- Lilja, Marianne, et al.
(author)
-
Liberation of free fatty acids during production of potato granules
- 1989
-
In: Food Chemistry. - : Elsevier BV. - 0308-8146 .- 1873-7072. ; 34:1, s. 15-23
-
Journal article (peer-reviewed)abstract
- The amount of free fatty acids and their composition were studied during an add-back process of potato granules. Samples were taken at several different stages in the production, from raw tubers to final potato granules. Lipids were extracted and lipid classes separated by liquid chromatography. Free fatty acids were separated from the neutral lipid fraction by high performance liquid chromatography (HPLC). The fatty acid composition was analysed by gas chromatography (GC). The amount of free fatty acid increased in the first stages of the process and rose to its highest level in the samples from the steam-cooking step. During further processing the amounts of free fatty acids slowly decreased. Since enzymatic hydrolysis is one explanation for liberation of fatty acids, lipase activity was measured by a spectrofluorimetric method in the raw tubers, blanched slices and steam-cooked slices. After the blanching step, some enzyme activity was found but after steam-cooking there was none. © 1989.
|
|
| 6. |
- Lilja, Marianne, et al.
(author)
-
Lipid changes during the production of potato granules
- 1989
-
In: Food Chemistry. - 0308-8146 .- 1873-7072. ; 31:4, s. 267-277
-
Journal article (peer-reviewed)abstract
- Potato granules were produced by an add-back-process. The lipid composition of the potato tubers and the final potato granules were assessed in order to study the influence of the process. The extracted lipids were fractionated into three major classes, neutral lipids, galacto-lipids and phospholipids, on a silicic acid column. The free fatty acids were separated from the neutral lipids by high performance liquid chromatography (HPLC). The fatty acid composition of the three lipid classes as well as the free fatty acid fraction was analysed by gas chromatography. No changes could be observed in the galactolipids and the phospholipids but the free fatty acid content was found to be about ten times higher in potato granules than in the potato tubers. © 1989.
|
|
| 7. |
- Lindmark, Bertil, et al.
(author)
-
The microheterogeneity of desialylated α1-antichymotrypsin : the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide
- 1989
-
In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. - : Elsevier BV. - 0167-4838. ; 997:1-2, s. 90-95
-
Journal article (peer-reviewed)abstract
- ACT (α1-antichymotrypsin), a serine antiproteinase with specificity against neutrophil cathepsin G, is homologous with α1-antitrypsin, plasminogen activator inhibitor and angiotensinogen, all with known amino-terminal microheterogeneity. Here we report that the two predominant isoforms of desialylated ACT obtained on isoelectric focusing correspond to a microheterogeneity at the amino terminus of ACT: one isoform (His-Pro-Asn-Ser-Pro-) and a two residues shorter isoform (Asn-Ser-Pro-). The relative occurrence of the two isoforms was comparable both in normal plasma, acute-phase plasma and plasma from subjects with heterozygous familial ACT deficiency. When desialyllated ACT, isolated by affinity chromatography from ACT-deficient, normal or acute-phase plasma, was compared with regard to mass and charge microheterogeneity, we found no significant differences in either respect. Nor was the isoform pattern of desialylated plasma from patients with rheumatoid arthritis different. Although the occurrence of heterozygous familial ACT deficiency implies genotypic variation, isolated ACT from patients with the trait was not found to exhibit any phenotypic variation detectable by standard electrophoretic methods.
|
|
| 8. |
- Lundwall, Åke, et al.
(author)
-
Molecular cloning of human prostate specific antigen cDNA
- 1987
-
In: FEBS Letters. - 1873-3468. ; 214:2, s. 22-317
-
Journal article (peer-reviewed)abstract
- A lambda gt11 clone encoding prostate specific antigen has been isolated from a human prostate cDNA library. The cDNA insert of 1415 nucleotides hybridizes specifically to a prostate mRNA species of 1.5 kb. The nucleotide sequence codes for part of a signal peptide, a short propiece and the mature protein of 237 amino acid residues. The Mr for the non-glycosylated protein was 26,089. One potential site for N-linked carbohydrate attachment was identified. The primary structure shows extensive homology with proteases of the kallikrein family.
|
|
| 9. |
- Ulvsbäck, M., et al.
(author)
-
Molecular cloning of a small prostate protein, known as beta-microsemenoprotein, PSP94 or beta-inhibin, and demonstration of transcripts in non-genital tissues
- 1989
-
In: Biochem Biophys Res Commun. ; 164:3, s. 5-1310
-
Journal article (peer-reviewed)abstract
- In order to study the gene expression of the seminal plasma protein beta-microseminoprotein, also known as PSP94 and beta-inhibin, clones encoding this protein were isolated from a cDNA library constructed in lambda gt11. Nucleotide sequencing confirmed the structure of a previously cloned cDNA. By northern blot analysis identical sized transcripts were demonstrated in the prostate, the respiratory (tracheal, bronchial and lung) tissues and the antrum part of the gastric mucosa. Thus, the protein is not primarily associated with male reproductive function. Although probably of no physiological significance, a slight structural similarity to the ovarian inhibin beta-chains was identified in the C-terminal half of the molecule.
|
|
