: Partial purification of phosphoenolpyruvate carboxykinase (PEPCK) from type 2 diabetic patients sera take place using some purification steps such as participation with ammonium sulphate (55-80%) and filtered through dialysis, then ion exchange chromatography by DEAE sepharose anion column, gel filtration chromatography by sephadex G-100 column. In ion exchange step, there are four peak are obtained, the highest enzyme activity obtained by (0.4 M Nacl) with purification fold (2.18), yield (44.3) of enzyme and specific activity (13.5) mg/ng, which obtained a single peak by gel filtration chromatography, the degree of purification (5.34) fold, yield of enzyme (20%) with specific activity (33.109mg/ng). The purified enzyme had an optimum tem

Lipase enzyme has attracted a lot of attention in recent years because of its diverse biotechnological applications. The present study was conducted to screen germinated seeds of four crops, namely sunflower (Helianthus annuus), flaxor linseed (Linum usitatissimum ), peanut (Arachis hypogaea  ) and castor bean (Ricinus communis), for the activity of their lipases. to the study also included the extraction and purification of lipase from the seeds of  the most promising crop using different solvents. The results indicated that the maximum enzymatic activity (0.669 U/ml) was  obtained when 0.1 M Tris-HCl buffer extract was used after 3 days of seed germination of all the tested species, as compared to the other test solvents

A protocol has been developed for micropropagation of Arachis hypogea L. under in
vitro conditions. Nodal explants gave rise to multiple shoots when cultured on MS medium
supplemented with different concentrations of BA (benzyladenine) with Kin (Kinetin) or GA3
(gibberellic acid). The highest response of shoot multiplication was obtained in MS
containing 1.5 mg.l¯¹ BA and 0.5 mg.L¯¹ Kin. The regenerated shootlets were rooted on MS
(Murashige and Skoog) basal medium with different concentrations of IBA (indolbutyric
acid) and IAA (indol acetic acid). The highest response of rooting was achieved with IBA at
0.05 + IAA at 0.05 mg.L¯¹. The maximum frequency of rooting and highest number of roots

This studay was performd on 30 serum specimens of patients having type II diabetes with cardiac disease, and 40 normal specimens were investigated as control group.The activity rate of AAP in patients (125.31± 3.28)I.U/L and activity rate of AAP in normals (6.76±2.21) I.U/L, in addition purification of AAP from serum patients having type II diabetes with cardiac diaease by using dialysis bag and gel filtration (Sephadex G-50). The results of the study reveal that Alanine aminopeptidase (AAP) activity of type II diabetes with cardiac disease patients' serum show a high signifiacant increase (p<0.001) compare to normal subject .

This study was performd on 50 urine specimens of patients with type 2 diabetes, in addition, 50 normal specimens were investigated as control group. The activity rate of maltase in patients (6.40±2.17) I.U/ml and activity rate of maltase in normal (0.44±0.20)I.U/ml. The results of the study reveal that maltase activity of type 2 diabetes patient's urine shows significant increase (P<0.01) compare to normal.

Forty one isolates of genus Proteus were collected from 140 clinical specimens such as urine, stool, wound, burn, and ear swabs from patients of both sex. These isolates were identified to three Proteus spp. P. mirabilis, P. vulgaris and P. penneri .The ability of these bacteria to produce L-asparaginase II by using semi quantitative and quantitative methods was determined. P. vulgaris Pv.U.92 was distinguished for high level of L-asparaginase II production with specific activity 1.97 U/mg. Optimum conditions for enzyme production were determined; D medium with 0.3% of L-asparagine at pH 7.5 with temperature degree 35°C for incubation. Ultrasonication was used to destroy the P. vulgaris Pv.U.92 cells then ASNase II was extracted and pu

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.