<b>Copyright information:</b>Taken from "Julius – a template based supplementary... more <b>Copyright information:</b>Taken from "Julius – a template based supplementary electronic health record system"http://www.biomedcentral.com/1472-6947/7/10BMC Medical Informatics and Decision Making 2007;7():10-10.Published online 2 May 2007PMCID:PMC1868711.
<b>Copyright information:</b>Taken from "Julius – a template based supplementary... more <b>Copyright information:</b>Taken from "Julius – a template based supplementary electronic health record system"http://www.biomedcentral.com/1472-6947/7/10BMC Medical Informatics and Decision Making 2007;7():10-10.Published online 2 May 2007PMCID:PMC1868711.
<b>Copyright information:</b>Taken from "Julius – a template based supplementary... more <b>Copyright information:</b>Taken from "Julius – a template based supplementary electronic health record system"http://www.biomedcentral.com/1472-6947/7/10BMC Medical Informatics and Decision Making 2007;7():10-10.Published online 2 May 2007PMCID:PMC1868711.
Background EHR systems are widely used in hospitals and primary care centres but it is usually di... more Background EHR systems are widely used in hospitals and primary care centres but it is usually difficult to share information and to collect patient data for clinical research. This is partly due to the different proprietary information models and inconsistent data quality. Our objective was to provide a more flexible solution enabling the clinicians to define which data to be recorded and shared for both routine documentation and clinical studies. The data should be possible to reuse through a common set of variable definitions providing a consistent nomenclature and validation of data. Another objective was that the templates used for the data entry and presentation should be possible to use in combination with the existing EHR systems. Methods We have designed and developed a template based system (called Julius) that was integrated with existing EHR systems. The system is driven by the medical domain knowledge defined by clinicians in the form of templates and variable definitio...
Biochemical and Biophysical Research Communications, 1986
The somatomedins insulin-like growth factor I and II (1,2) are in serum bound to high-molecular w... more The somatomedins insulin-like growth factor I and II (1,2) are in serum bound to high-molecular weight binding proteins (6,7,8). By use of a four step chromatographic procedure a somatomedin binding protein was isolated from outdated human plasma. Exclusion chromatography on Sephadex G-200 disclosed a molecular weight of 150 kDa. After lyophilization however, the binding activity was found in a lower molecular weight range of 35-45 kDa. A partial amino acid sequence analysis of the lyophilized material revealed a possible N-terminal sequence of Ala-Pro-Trp. This sequence is identical to the N-terminal sequence of the 35 kDa somatomedin binding protein previously isolated from human amniotic fluid (16).
Ion-exchange chromatography of serum on DEAE-Sephadex A-50 using a stepwise NaCl gradient showed ... more Ion-exchange chromatography of serum on DEAE-Sephadex A-50 using a stepwise NaCl gradient showed that complexes enriched with insulin-like growth factors I and II (IGF-I and IGF-II) could be preferentially eluted. A fraction eluted with 0.075 M-NaCl preferentially contained immunoreactive IGF-I with peak levels appearing in fractions of Mr approx. 110,000. The IGF-I-binding protein complex itself had low bioactivity as measured in a non-suppressible insulin-like (NSILA) bioassay. On conversion to free IGF-I by gel-permeation chromatography on Sephadex G-75 in 1% formic acid, however, the IGF-I did express its intrinsic NSILA bioactivity. In contrast, an IGF-II-enriched complex was eluted from the DEAE-Sephadex with 0.15 M-NaCl. Practically all of the recovered NSILA of the original serum was present in this fraction, in the Mr range 70,000-300,000 with a peak of 150,000. Chromatography on Sephadex G-75 in 1% formic acid separated this high-Mr NSILA into low-Mr (less than 15000) IGF-...
The polypeptide termed somatomedin A (SMA) was isolated from outdated human plasma by a new purif... more The polypeptide termed somatomedin A (SMA) was isolated from outdated human plasma by a new purification procedure, not using acid ethanol extraction. Fractions containing SMA were monitored by a placenta radioreceptorassay and a radioimmunoassay for SMA. The purification method utilized a microcomputer-controlled chromatography system, yielding both SMA (identified as insulin-like growth factor 1 (IGF-1) or a deamidated derivative) and insulin-like growth factor 2 (IGF-2). The first step of CM-Affigel blue adsorbed at neutral pH the majority of somatomedins detectable by the radioreceptorassay for SMA. Exclusion chromatography on Sephadex G-50 in 0.1 M acetic acid separated this active material from albumin and NaCl. Separation between SMA and IGF-2 was achieved on two different cation-exchange columns, but not in the final high-performance liquid chromatography step. The isoelectric points, determined by chromatofocusing, were 8.0 for SMA and 6.2 for IGF-2. The amino acid compositions of the two isolated peptides were indistinguishable from the known compositions of IGF-1 and IGF-2. Sequence analysis up to position 39 of the peptide with a pI of 6.2 also proved identity with IGF-2 for all positions examined. The peptide with a pI of 8.0, corresponding to SMA, was degraded directly as well as after CNBr cleavage. The results show that it is identical to IGF-1, with the possible exception of acid/amide assignment, which could correspond to a deamidation. If occurring in the native preparation before analysis, it could explain the chromatographic properties and isoelectric point of SMA versus IGF-1 isolated by other techniques.
A homologous radioreceptor assay (RRA) has been developed for Insulin-like Growth Factor II (IGF ... more A homologous radioreceptor assay (RRA) has been developed for Insulin-like Growth Factor II (IGF II) using the human erythroleukemia cell line K562. These cells have binding sites for insulin and IGF-II but not for Insulin-like Growth Factor I (IGF I). All samples were dissociated and separated from binding proteins by gel filtration at acidic pH. In healthy adults the mean serum level of radioreceptor assayable IGF II (RRA-IGF II) and 95% confidence limits were 965 ng/ml and 717-1299 ng/ml, respectively. The mean level in GH deficient patients was significantly lower (p less than 0.001) compared with healthy subjects whereas no change was found in patients with acromegaly and uremia. Slightly lowered levels of RRA-IGF II were found in one patient with a tumor induced hypoglycemia.
The Journal of Clinical Endocrinology & Metabolism, 1984
Somatomedin (Sm) levels throughout pregnancy were determined in a longitudinal study of four norm... more Somatomedin (Sm) levels throughout pregnancy were determined in a longitudinal study of four normal women and three patients with GH deficiency by use of the RIA for Sm-A, a newly developed RIA for insulin-like growth factor 2 (IGF-2), and the placenta RRA for Sm-A. In both normal women and those with GH deficiency, there was a continuous rise of immunoreactive Sm-A throughout pregnancy. During the third trimester the levels were 2-fold elevated above the level in nonpregnant age-matched normal subjects. No change of immunoreactive IGF-2 levels was found in the normal pregnant women, whereas an increase from low to normal levels was found in GH-deficient patients during pregnancy. The placenta RRA-Sm-A did not detect the increase of Sm-A immunoactivity in the normal pregnant women, whereas the levels were normalized in GH-deficient patients. After delivery a rapid fall of Sm levels occurred in patients with GH deficiency. The calculated half-lives for immunoreactive Sm-A and IGF-2 were 27 and 52 h, respectively. The birth weights of the seven children were significantly (P less than 0.05) correlated to both the individual peak and the mean maternal value of immunoreactive Sm-A during the last trimester. The present findings indicate that the production of both IGF-1 and IGF-2 related peptides during pregnancy is independent of maternal pituitary GH production.
The Journal of Clinical Endocrinology & Metabolism, 1979
A RIA has been developed for somatomedin A (SM-A) utilizing Sepharose-bound antibodies. This assa... more A RIA has been developed for somatomedin A (SM-A) utilizing Sepharose-bound antibodies. This assay, measuring SM-A, the insulin-like growth factors 1 and 2, and somatomedin C, allows determination in serum samples. In comparison with a serum standard, the mean serum levels in patients with acromegaly or GH deficiency and healthy subjects were 8.7 %/- 0.7 (n = 25), 0.24 +/- 0.02 (n = 25), and 1.15 +/- 0.11 U/ml, respectively. The correlation coefficient between immunoreactive SM-A and SM-A by radioreceptor assay was highly significant (r = 0.93), although the potency ratio of SM-A between the two groups of patients was higher in the RIA than in the radioreceptor assay. Gel chromatography revealed that SM-A in acromegalic serum is bound to a carrier protein which is absent in patients with GH deficiency. After gel chromatography at low pH, 90% of applied immunoreactive SM-A was recovered in the low molecular weight fraction and consisted mainly of neutral polypeptides.
<b>Copyright information:</b>Taken from "Julius – a template based supplementary... more <b>Copyright information:</b>Taken from "Julius – a template based supplementary electronic health record system"http://www.biomedcentral.com/1472-6947/7/10BMC Medical Informatics and Decision Making 2007;7():10-10.Published online 2 May 2007PMCID:PMC1868711.
<b>Copyright information:</b>Taken from "Julius – a template based supplementary... more <b>Copyright information:</b>Taken from "Julius – a template based supplementary electronic health record system"http://www.biomedcentral.com/1472-6947/7/10BMC Medical Informatics and Decision Making 2007;7():10-10.Published online 2 May 2007PMCID:PMC1868711.
<b>Copyright information:</b>Taken from "Julius – a template based supplementary... more <b>Copyright information:</b>Taken from "Julius – a template based supplementary electronic health record system"http://www.biomedcentral.com/1472-6947/7/10BMC Medical Informatics and Decision Making 2007;7():10-10.Published online 2 May 2007PMCID:PMC1868711.
Background EHR systems are widely used in hospitals and primary care centres but it is usually di... more Background EHR systems are widely used in hospitals and primary care centres but it is usually difficult to share information and to collect patient data for clinical research. This is partly due to the different proprietary information models and inconsistent data quality. Our objective was to provide a more flexible solution enabling the clinicians to define which data to be recorded and shared for both routine documentation and clinical studies. The data should be possible to reuse through a common set of variable definitions providing a consistent nomenclature and validation of data. Another objective was that the templates used for the data entry and presentation should be possible to use in combination with the existing EHR systems. Methods We have designed and developed a template based system (called Julius) that was integrated with existing EHR systems. The system is driven by the medical domain knowledge defined by clinicians in the form of templates and variable definitio...
Biochemical and Biophysical Research Communications, 1986
The somatomedins insulin-like growth factor I and II (1,2) are in serum bound to high-molecular w... more The somatomedins insulin-like growth factor I and II (1,2) are in serum bound to high-molecular weight binding proteins (6,7,8). By use of a four step chromatographic procedure a somatomedin binding protein was isolated from outdated human plasma. Exclusion chromatography on Sephadex G-200 disclosed a molecular weight of 150 kDa. After lyophilization however, the binding activity was found in a lower molecular weight range of 35-45 kDa. A partial amino acid sequence analysis of the lyophilized material revealed a possible N-terminal sequence of Ala-Pro-Trp. This sequence is identical to the N-terminal sequence of the 35 kDa somatomedin binding protein previously isolated from human amniotic fluid (16).
Ion-exchange chromatography of serum on DEAE-Sephadex A-50 using a stepwise NaCl gradient showed ... more Ion-exchange chromatography of serum on DEAE-Sephadex A-50 using a stepwise NaCl gradient showed that complexes enriched with insulin-like growth factors I and II (IGF-I and IGF-II) could be preferentially eluted. A fraction eluted with 0.075 M-NaCl preferentially contained immunoreactive IGF-I with peak levels appearing in fractions of Mr approx. 110,000. The IGF-I-binding protein complex itself had low bioactivity as measured in a non-suppressible insulin-like (NSILA) bioassay. On conversion to free IGF-I by gel-permeation chromatography on Sephadex G-75 in 1% formic acid, however, the IGF-I did express its intrinsic NSILA bioactivity. In contrast, an IGF-II-enriched complex was eluted from the DEAE-Sephadex with 0.15 M-NaCl. Practically all of the recovered NSILA of the original serum was present in this fraction, in the Mr range 70,000-300,000 with a peak of 150,000. Chromatography on Sephadex G-75 in 1% formic acid separated this high-Mr NSILA into low-Mr (less than 15000) IGF-...
The polypeptide termed somatomedin A (SMA) was isolated from outdated human plasma by a new purif... more The polypeptide termed somatomedin A (SMA) was isolated from outdated human plasma by a new purification procedure, not using acid ethanol extraction. Fractions containing SMA were monitored by a placenta radioreceptorassay and a radioimmunoassay for SMA. The purification method utilized a microcomputer-controlled chromatography system, yielding both SMA (identified as insulin-like growth factor 1 (IGF-1) or a deamidated derivative) and insulin-like growth factor 2 (IGF-2). The first step of CM-Affigel blue adsorbed at neutral pH the majority of somatomedins detectable by the radioreceptorassay for SMA. Exclusion chromatography on Sephadex G-50 in 0.1 M acetic acid separated this active material from albumin and NaCl. Separation between SMA and IGF-2 was achieved on two different cation-exchange columns, but not in the final high-performance liquid chromatography step. The isoelectric points, determined by chromatofocusing, were 8.0 for SMA and 6.2 for IGF-2. The amino acid compositions of the two isolated peptides were indistinguishable from the known compositions of IGF-1 and IGF-2. Sequence analysis up to position 39 of the peptide with a pI of 6.2 also proved identity with IGF-2 for all positions examined. The peptide with a pI of 8.0, corresponding to SMA, was degraded directly as well as after CNBr cleavage. The results show that it is identical to IGF-1, with the possible exception of acid/amide assignment, which could correspond to a deamidation. If occurring in the native preparation before analysis, it could explain the chromatographic properties and isoelectric point of SMA versus IGF-1 isolated by other techniques.
A homologous radioreceptor assay (RRA) has been developed for Insulin-like Growth Factor II (IGF ... more A homologous radioreceptor assay (RRA) has been developed for Insulin-like Growth Factor II (IGF II) using the human erythroleukemia cell line K562. These cells have binding sites for insulin and IGF-II but not for Insulin-like Growth Factor I (IGF I). All samples were dissociated and separated from binding proteins by gel filtration at acidic pH. In healthy adults the mean serum level of radioreceptor assayable IGF II (RRA-IGF II) and 95% confidence limits were 965 ng/ml and 717-1299 ng/ml, respectively. The mean level in GH deficient patients was significantly lower (p less than 0.001) compared with healthy subjects whereas no change was found in patients with acromegaly and uremia. Slightly lowered levels of RRA-IGF II were found in one patient with a tumor induced hypoglycemia.
The Journal of Clinical Endocrinology & Metabolism, 1984
Somatomedin (Sm) levels throughout pregnancy were determined in a longitudinal study of four norm... more Somatomedin (Sm) levels throughout pregnancy were determined in a longitudinal study of four normal women and three patients with GH deficiency by use of the RIA for Sm-A, a newly developed RIA for insulin-like growth factor 2 (IGF-2), and the placenta RRA for Sm-A. In both normal women and those with GH deficiency, there was a continuous rise of immunoreactive Sm-A throughout pregnancy. During the third trimester the levels were 2-fold elevated above the level in nonpregnant age-matched normal subjects. No change of immunoreactive IGF-2 levels was found in the normal pregnant women, whereas an increase from low to normal levels was found in GH-deficient patients during pregnancy. The placenta RRA-Sm-A did not detect the increase of Sm-A immunoactivity in the normal pregnant women, whereas the levels were normalized in GH-deficient patients. After delivery a rapid fall of Sm levels occurred in patients with GH deficiency. The calculated half-lives for immunoreactive Sm-A and IGF-2 were 27 and 52 h, respectively. The birth weights of the seven children were significantly (P less than 0.05) correlated to both the individual peak and the mean maternal value of immunoreactive Sm-A during the last trimester. The present findings indicate that the production of both IGF-1 and IGF-2 related peptides during pregnancy is independent of maternal pituitary GH production.
The Journal of Clinical Endocrinology & Metabolism, 1979
A RIA has been developed for somatomedin A (SM-A) utilizing Sepharose-bound antibodies. This assa... more A RIA has been developed for somatomedin A (SM-A) utilizing Sepharose-bound antibodies. This assay, measuring SM-A, the insulin-like growth factors 1 and 2, and somatomedin C, allows determination in serum samples. In comparison with a serum standard, the mean serum levels in patients with acromegaly or GH deficiency and healthy subjects were 8.7 %/- 0.7 (n = 25), 0.24 +/- 0.02 (n = 25), and 1.15 +/- 0.11 U/ml, respectively. The correlation coefficient between immunoreactive SM-A and SM-A by radioreceptor assay was highly significant (r = 0.93), although the potency ratio of SM-A between the two groups of patients was higher in the RIA than in the radioreceptor assay. Gel chromatography revealed that SM-A in acromegalic serum is bound to a carrier protein which is absent in patients with GH deficiency. After gel chromatography at low pH, 90% of applied immunoreactive SM-A was recovered in the low molecular weight fraction and consisted mainly of neutral polypeptides.
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