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| 2. |
- Lohmander, Stefan, et al.
(author)
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Chemical and metabolic heterogeneity of chondroitin sulfate and keratan sulfate in guinea pig cartilage and nucleus pulposus
- 1973
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In: Biochimica et Biophysica Acta. General Subjects. - : Elsevier BV. - 0304-4165. ; 304:2, s. 430-448
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Journal article (peer-reviewed)abstract
- Chondroitin sulfate and keratan sulfate in guinea pig costal cartilage, nasal septum cartilage and nucleus pulposus were separated and fractionated by chromatography on CPC-cellulose, ECTEOLA-cellulose and Sephadex G-200 columns. Characterization of the chondroitin sulfates included determination of molecular weight and of the number, and position, of sulfate groups of the disaccharide units. Distinct chemical differences were found between the total fractions of chondroitin sulfate from the three tissues. Within the total fractions a marked heterogeneity was also apparent. The turnover of the two glycosaminoglycans was studied by using radioactive sulfate as precursor. The guinea pigs were killed at eight intervals, ranging from 30 min to 40 days after injection of the isotope. Total fractions of chondroitin sulfate from rib, nasal septum and nucleus pulposus showed half-lives of about 80, 40 and 30 days, respectively. In addition, the existence of a second metabolic component with a faster turnover (half-life about 3 days) was indicated in chondroitin sulfate from all three tissues. Similarly, keratan sulfate from the rib contained a 'slow' component with a half-life of about 90 days and a 'fast' component with a half-life of 4 days. For keratan sulfate from nucleus pulposus only a single component was demonstrable; it had a half-life of about 30 days. Within the total fractions of both chondroitin sulfate and keratan sulfate from the three tissues studied, a considerable degree of metabolic heterogeneity was apparent between, and within, subfractions of differing molecular weight.
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| 3. |
- Lohmander, Stefan
(author)
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Ion exchange chromatography of glucosamine and galactosamine in microgram amounts with quantitative determination and specific radioactivity assay
- 1972
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In: Biochimica et Biophysica Acta. General Subjects. - : Elsevier BV. - 0304-4165. ; 264:3, s. 411-417
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Journal article (peer-reviewed)abstract
- A rapid method for the separation and quantitative determination, including radioassay, of glucosamine and galactosamine in microgram amounts is described. It is based upon the use of a column of Aminex A-5 ion exchange resin eluted with a phosphate buffer at pH 7.00 and 60 °C. From each fraction half the volume is used for a scaled down Elson-Morgan procedure and other half for liquid scintillation counting. Amounts of about 0.01-1 μmole of hexosamine may be separated and determined.
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| 4. |
- Lohmander, Stefan, et al.
(author)
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Proteoglycans of mineralizing rib and epiphyseal cartilage
- 1975
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In: Biochimica et Biophysica Acta. General Subjects. - : Elsevier BV. - 0304-4165. ; 404:1, s. 93-109
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Journal article (peer-reviewed)abstract
- Rib cartilage from growing guinea pigs and epiphyseal cartilage from Beagle puppie were separated into three fractions, representing non-mineralized, low mineralized, and high mineralized, tissue, by centrifuging finely ground material in acetone/bromoform density gradients. Following extraction under dissociative conditions, the proteoglycans were fractionated by density gradient ultracentrifugation under associative and dissociative conditions. With the onset of mineralization, the cartilage lost approximately half its content of proteoglycans. The proteoglycans remaining in the calcified cartilage differed in composition and in size from those of nonmineralized tissue. With the increased mineral content of the tissues the ratios of protein to polysaccharide, of chondroitin sulfate to keratan sulfate, and of 4-sulfated to 6-sulfated chondroitin sulfate increased in the proteoglycan fraction. Furthermore, gel chromatograms indicated decreased proportions of very high molecular weight proteoglycans, in mineralized tissue.
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| 5. |
- Tejler, L, et al.
(author)
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Production of protein HC by human fetal liver explants
- 1978
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In: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002 .- 0304-4165. ; 542:3, s. 14-506
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Journal article (peer-reviewed)abstract
- Human fetal lever explants were found to secrete protein HC into the medium in molar amounts comparable to those of albumin, alpha 1-antitrypsin and orosomucoid. Incorporation of a radioactive amino acid from the medium into the secreted protein HC demonstrated de novo synthesis. The secreted protein HC had the same size and electrophoretic mobility as protein HC of plasma and urine and gave a reaction of immunochemical identity with the protein in these biological fluids.
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| 6. |
- Dahlqvist, Ulla, et al.
(author)
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Endogenous substrates of protein kinase in rat liver cell sap under different dietary conditions
- 1978
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In: Biochimica et Biophysica Acta. - : Elsevier BV. - 0006-3002 .- 1878-2434 .- 0304-4165. ; 540:1, s. 13-23
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Journal article (peer-reviewed)abstract
- Liver cell sap from normally fed rats, rats fed with a high-carbohydrate diet and fasted rats was chromatographed on DEAE-cellulose (pH 7.0). The chromatogram from each diet group was analyzed for pyruvate kinase activity and endogenous substrates of cyclic AMP-stimulated protein kinase. The materials were pooled into five phosphorylatable fractions, in each of which phosphate incorporation at 0.1 mM and 1.0 mM [32P]ATP in the presence of cyclic AMP and protein kinase was determined. For characterization of the phosphorylatable components, thin-layer gel chromatography on Sephadex G-200 and polyacrylamide gel electrophoresis in detergent were used for determination of native and minimal molecular weights, respectively. Except for pyruvate kinase, eight components which incorporated at least 0.05 nmol of [32P]phosphate/g of liver were detected. The phosphorylation of four of them was stimulated by cyclic AMP. Their minimal molecular weights were 42000, 21000, 52000 and 49000. The component with a minimal molecular weight of 42000 seemed to have a native molecular weight of 160000. Both the 21000 and the 52000 component had a native molecular weight of about 110000-120000. The protein with a minimal molecular weight of 49000 could not be correlated with certainty to a native molecular weight. The proteins whose phosphorylation was not stimulated by cyclic AMP had minimal molecular weights of 54000, 39000, 34000 and 22000.
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| 7. |
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| 8. |
- Mattiasson, Bo, et al.
(author)
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Studies on a matrix-bound three-enzyme system.
- 1971
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In: Biochimica et Biophysica Acta - General Subjects. - : Elsevier BV. - 0304-4165 .- 0005-2744. ; 235:1, s. 253-257
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Journal article (peer-reviewed)
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