| 1. |
- Henricsson, M., et al.
(författare)
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The frequency and severity of retinopathy are related to HbA(1c) values after, but not at, the diagnosis of NIDDM
- 1998
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Ingår i: Journal of Internal Medicine. - : Wiley. - 0954-6820 .- 1365-2796. ; 244:2, s. 149-154
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Tidskriftsartikel (refereegranskat)abstract
- Objectives. To examine the relationship between previous glycaemic exposure and prevalence of retinopathy 8 years after diagnosis of diabetes in 58 islet cell antibodies (ICA)-negative noninsulin-dependent diabetes mellitus (NIDDM) patients and in a group of 14 ICA-positive 'NIDDM' and insulin-dependent diabetes mellitus (IDDM) patients. Design and methods. The Wisconsin retinopathy scale was used to assess the retinopathy which was graded into mild, moderate and severe nonproliferative diabetic retinopathy (NPDR), or proliferative retinopathy (PDR). The frequency and severity of retinopathy was related to HbA(1c) levels at diagnosis, and 3 and 5 years later. Results. Thirty of the 58 ICA-negative NIDDM patients (52%) but only 2 of the 14 ICA-positive 'NIDDM' or IDDM patients (14%) had mild-moderate- severe NPDR 8 years after diagnosis (P = 0.02). None had PDR. Retinopathy 8 years after diagnosis in NIDDM (= 58 ICA-negative patients) was correlated with the degree of glycaemiC control (HbA(1c) levels) at 3 and 5 years after diagnosis, but not to HbA(1c) levels at diagnosis. The relative risk for a higher average HbA(1c) (per percentage) at 3 and 5 years was 1.56 for any retinopathy vs. no retinopathy (95% confidence interval 1.1-2.2; P = 0.01) and 1.68 for moderate to severe NPDR in comparison with no DR and mild NPDR (95% confidence interval 1.0-2.8; P = 0.04). Conclusions. Retinopathy after 8 years of diabetes in NIDDM patients was associated with impaired glycaemic control during previous years but not with glycaemic control at baseline. Good glycaemic control may prevent retinopathy in patients with NIDDM.
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| 2. |
- Lilja, H., et al.
(författare)
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Amino acid sequence of the predominant basic protein in human seminal plasma
- 1985
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Ingår i: FEBS Letters. - : Wiley. - 0014-5793. ; 182:1, s. 181-184
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Tidskriftsartikel (refereegranskat)abstract
- The predominant basic protein in liquefied human seminal plasma is the major degradation product of the gel-forming protein secreted by the seminal vesicles. The amino acid sequence of this basic protein is presented. The basic protein contains 52 amino acid residues. It is devoid of cysteine, methionine, tryptophan, and leucine, but contains seven histidine residues located in the NH2-terminal half of the molecule. The calculated Mr of 5753 is in close agreement with that obtained from gel filtration in guanidine-HCl on Sephacryl S-200(Mr = 6000).
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| 3. |
- Lilja, H., et al.
(författare)
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Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein
- 1984
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 44:5, s. 439-446
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Tidskriftsartikel (refereegranskat)abstract
- From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose® chromatography was followed by gel filtration (Biogel® P 60) and by fast performance liquid chromatography on a reversed phase column (C8). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a PI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the protein sequence is unique: HNKQEGRDHDKSKG HFHRVVIHHKGGKAHRG-.A specific rabbit antiserum was raised against the 12.8 kDa basic protein. The protein was found to be unique to seminal plasma among all extracellular fluids examined. Three immunologically related 52 kDa, 71 kDa, and 76 kDa proteins were identified in seminal vesicle secretion when it had been reduced. Prostatic enzyme(s) degraded these proteins to the 12.8 kDa basic protein and several other basic proteins with apparent molecular masses below 18 kDa.
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| 4. |
- Lilja, H., et al.
(författare)
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Evaluation of serum γ-glutamyltransferase by electrofocusing, and variations in isoform patterns
- 1983
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Ingår i: Clinical Chemistry. - : Oxford University Press (OUP). - 0009-9147 .- 1530-8561. ; 29:6, s. 1034-1037
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Tidskriftsartikel (refereegranskat)abstract
- Serum γ-glutamyltransferase (EC 2.3.2.2) showed microheterogeneity on electrofocusing, owing to variations in sialic acid content. We investigated the isoform patterns of papain-treated serum samples on agarose gels containing nonionic detergent and ampholytes in the low pH range. Serum from cases of cholestasis show seven bands with γ-glutamyltransferase activity. These same bands were also found in liver tissue similarly treated, and they had pl values ranging from 3.8 to 4.2. Papain-treated sera that also had been neuraminidase digested showed only a single band, still enzymatically active and with a pI of 5.9. Increased γ-glutamyltransferase in serum as a result of alcoholic abuse was combined with a abnormally high degree of sialylation of the enzyme, giving more anodal isoforms. The decline in the concentration of this enzyme during several weeks of abstinence was accompanied by a gradual decrease in γ-glutamyltransferase sialylation and the appearance of more cathodal fractions.
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