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H Jacobsen

Publications and source records attributed to H Jacobsen.

99 records · Page 6Linked to original sources
PubMed1977

Sequence analysis of porcine gut GLI-1.

A protein from porcine gut with 100 amino acid residues (porcine gut GLI-1) and having glucagon-like immunoreactivity has been characterized by partial sequences. The sequence of the C-terminal amino acid residues is -Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala and includes the C-terminal amino acid residue sequence (-Met-Asn-Thr) of porcine glucagon. Evidence is presented that the glucagon sequence -Thr-Ser-Asp-Tyr-Ser-Lys-Tyr- is found in the gut GLI-1 as well. The data support the theory that gut GLI-1 contains the full glucagon sequence and that gut GLI-1 and glucagon are formed from a common precursor.

Amino Acid Sequence↗
PubMed1977

The complete amino acid sequence of prochymosin.

The total sequence of 365 amino acid residues in bovine prochymosin is presented. Alignment with the amino acid sequence of porcine pepsinogen shows that 204 amino acid residues are common to the two zymogens. Further comparison and alignment with the amino acid sequence of penicillopepsin shows that 66 residues are located at identical positions in all three proteases. The three enzymes belong to a large group of proteases with two aspartate residues in the active center. This group forms a family derived from one common ancestor.

Amino Acid Sequence↗
PubMed1976

Structure-function relationship: immunologic.

It is suggested that the antigenic site of glucagon for the specific sera is located within the 24-29 section of the molecule and within the 2-23 section for the fully cross-reacting sera. Biologically inactivated glucagon may retain immunoreactivity in spite of the loss of receptor-binding activity.

Animals↗
PubMed1976

Purification and characterization of a protein from porcine gut with glucagon-like immunoreactivity.

A protein with glucagon-like immunoreactivity has been isolated from porcine intestine in a highly purified form. The isoelectric point is 6.8-6.9, and the molecular weight is 11,625, as calculated from its amino acid composition: this estimate has been confirmed by S.D.S. gel electrophoresis. The partial sequence so far elucidated is from the N-terminal: Arg-Ser-Leu-Gin-Asn-Thr-Glx-Glx-Lys-Ala-Arg-Ser-Phe-, and from the C-terminal: -Ile-Ala, both differing from those of porcine pancreatic glucagon. On a molar basis the protein has the same immunoreactivity as porcine glucagon when assayed with some anti-glucagon sera, while the activity is less than 0.2% using other anti-glucagon sera.

Amino Acid Sequence↗
PubMed1975

[Poor nursing care].

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Nurse-Patient Relations↗
PubMedDate not supplied

Antiviral effects of recombinant tumour necrosis factor in vitro.

Tumour necrosis factor (TNF) was first described as a factor in the serum of mice injected with tubercle bacilli (BCG) and several days later with lipopolysaccharide (LPS). The gene encoding TNF has recently been cloned and pure recombinant human TNF is now available. TNF is known for its in vivo antitumour effect and in vitro cytotoxicity on certain transformed cell lines. Similarities in amino acid sequence and biological activity to lymphotoxin and cachectin have been reported, and very recently a growth-factor-like activity on diploid fibroblasts was observed. There is no similarity between these proteins and interferons (IFNs), which are also induced during in vivo induction of TNF. Here we describe the antiviral activity of pure recombinant human TNF in a typical in vitro antiviral assay which we discovered while investigating the possible role of TNF as an inducer of IFN.

2',5'-Oligoadenylate Synthetase↗
PubMedDate not supplied

[Interferons--biologic principles and clinical uses].

Interferons are components of the nonspecific defense system. Their most prominent biological roles are the antiviral, the antiproliferative, and the immunoregulatory activities. However, their primary functions within the organism remains to be determined. Three types of IFNs have been described so far (IFN alpha, IFN beta, IFN gamma). They possess similar but not necessarily identical biological activity. Interferons resemble peptide hormones and growth factors in that they bind to receptors on the cell surface, exert their activity through a postulated "second messenger" and are effective at picomolar concentrations. Interferons have been used as therapeutic agents in viral and malignant diseases with encouraging results in some patients. However, in only few instances interferon may become the standard therapeutic regimen. Since novel therapeutic approaches for cancer and viral disease are urgently needed, additional clinical trials with interferons seem to be justified. These have become feasible because sufficient amounts of pure interferon are available by novel production techniques based on modern biotechnology.

Cell Division↗
PubMedDate not supplied

Use of a sicca symptoms questionnaire for the identification of patients with Sjögren's syndrome in a heterogeneous hospital population with various rheumatic diseases.

OBJECTIVE: A six-item questionnaire regarding sicca symptoms recently validated for primary Sjögren's syndrome (SS) was tested on 154 in-patients with a wide range of inflammatory rheumatic diseases. Patients with one or more positive responses underwent objective ocular and oral diagnostic procedures. Of 27 patients thus investigated, 19 could be classified as having SS. RESULTS: The positive answers obtained were mainly in response to 4 of the 6 questions: dry eyes, sensation of sand or gravel in the eyes, dry mouth, and drinking of liquids to aid in swallowing dry foods. Among the 19 patients found with SS, most had had earlier diagnoses of various connective tissue diseases (rheumatoid arthritis included) and most were female. CONCLUSION: In conclusion, this study indicates that the sicca symptom questionnaire may be useful when deciding which patients with inflammatory rheumatic diseases should be subjected to special investigations with regard to SS.

Aged↗