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Biomedical subjects

T Holm

Publications and source records attributed to T Holm.

At least 73 records · Page 4Linked to original sources

C-reactive protein in tibial fractures. Natural response to the injury and operative treatment.

Serial serum C-reactive protein (CRP) measurements were made, for three weeks, in 42 consecutive patients with solitary tibial fractures. The CRP response was related to the treatment: lower values were observed in 27 patients treated conservatively than in 15 operated patients. Open reduction and plating resulted in a greater response than closed intramedullary nailing. The timing of the CRP response was related to the timing of the treatment: the highest values were usually recorded two days after admission or operation. The timing of the operation did not affect the degree of CRP response. Neither the site, nor the type of fracture, nor the age of the patient played any role. Awareness of these natural CRP responses after fractures may help in the diagnosis of early post-traumatic and postoperative complications, especially infections.

Adolescent↗

Members of the RTVL-H family of human endogenous retrovirus-like elements are expressed in placenta.

A cDNA clone homologous to the RTVL-H family of human retrovirus-like elements was isolated from a human placenta cDNA library. The nucleotide sequence of the 1084-bp cDNA revealed an open reading frame (ORF) that may encode a 146 amino acid protein with significant homology to retroviral proteases. Downstream from the putative protease ORF a 3' long terminal repeat (LTR) containing U3 and R regions was found. The cDNA sequence ends in a poly(A) tail appropriately positioned downstream from a polyadenylation signal in the LTR. Northern-blot analysis showed that several distinct RTVL-H homologous transcripts are present in human placenta. We also show that repetitive RTVL-H homologous sequences are present in the genomes of both gorilla and African green monkey.

Amino Acid Sequence↗

Cloning and sequencing of the gene encoding the phosphatidylcholine-preferring phospholipase C of Bacillus cereus.

A synthetic oligodeoxynucleotide probe was used to clone the gene encoding the phosphatidylcholine-preferring phospholipase C of Bacillus cereus. The sequence of a 2050-bp restriction fragment containing the gene was determined. Analysis of the gene-derived amino acid (aa) sequence showed that this exoenzyme is probably synthesized as a 283-aa precursor with a 24-aa signal peptide and a 14-aa propeptide. The mature, secreted enzyme comprises 245 aa residues. Sonicates of Escherichia coli HB101 carrying the gene on a multicopy plasmid showed phospholipase C activity. This activity was inhibited by Tris, a known inhibitor of the B. cereus enzyme and also by antiserum raised against pure B. cereus phospholipase C. We conclude therefore that the gene is expressed in E. coli. The cloning and sequencing described here complete the first step toward using in vitro mutagenesis for investigations of the structure-function relationships of B. cereus phospholipase C.

Amino Acid Sequence↗